CURRICULUM VITAE
`Vincent A. Fischetti, Ph.D.
`Rockefeller University
`1230 York Avenue
`New York, NY 10021
`Pho: 212-327-8166
`Fax: 212-327-7584
`Cell: 516-901-8400
`E-mail: vaf@rockefeller.edu
`Web site: www.rockefeller.edu/vaf
`Personal: Married with 2 adult children
`Education: Ph.D. New York University School of Medicine, Microbiology, 1970, (honors)
`M.S. Long Island University, Microbiology, 1967
`B.S. Wagner College, Bacteriology, 1962
`Training and Experience:
`1990 -Pres. Professor and Chairman, Laboratory of Bacterial Pathogenesis and
`Immunology, The Rockefeller University, New York, N.Y.
`1978 - 1990 Associate Professor, The Rockefeller University, New York, N.Y.
`1973 - 1978 Assistant Professor, The Rockefeller University, New York, N.Y.
`1970 - 1979 Adjunct Assistant Professor, Adelphi University, Garden City, N.Y.
`1972 - 1973 Guest Investigator, The Rockefeller University, New York, N.Y.
`1972 - 1973 Postdoctoral Fellow, Albert Einstein College of Medicine, N.Y.
`1970 - 1972 Postdoctoral Fellow, The Rockefeller University, New York, N.Y.
`Membership:
`American Society for Microbiology
`American Academy for Microbiology
`National Academy of Inventors
`Honors and Awards (selected):
`
`2019
`2019
`2017
`2017
`2016
`2015
`2014
`2013
`2013
`2013
`2012
`2012
`2011
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`Invited speaker, IDWeek, Washington DC
`Invited speaker for IPATH Seminar Series, UCSD
`Distinguished Lecturer in Medical Sciences, U. of Oklahoma School of Med
`Grand Rounds, Memorial Sloan Kettering Cancer Center, NY
`Elected as a Fellow, National Academy of Inventors
`Wellcome Trust committee on Alternatives to Antibiotics
`Invited Speaker - ICAAC
`Medical Grand Rounds, Mt. Sinai School of Medicine, NY
`Keynote Speaker, Medimmune Science Retreat, Maryland
`Keynote Speaker, Int. Symposia, MRSA in Farm Animals, Copenhagen
`Marie Curie Guest Lecturer, Copenhagen, Denmark
`Medical Grand Rounds, Weill Cornell Medical College, NY
`Distinguished Lecturer in Biomedical Science, Harvard University, Boston MA
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`Keynote address, Phage 2011, Oxford England
`2011
`Edwin H. Beachey Distinguished Visiting Professorship, UT, Memphis
`2011
`Keynote address, Dutch Infectious Diseases Update Course, Amsterdam
`2011
`Invited Speaker, Institute Pasteur Phage Symposium
`2010
`Honorary Doctor of Science, Wagner College, Staten Island, NY
`2010
`Invited Speaker, Nobel Symposium – Sweden ”Gram-Positive Infections”
`2009
`Distinguished Nelson Lecturer, University of Montana
`2009
`Speaker: Royal Society London,” Tackling antibacterial resistance”
`2008
`Keynote Speaker, Edinburgh International Phage Conference
`2008
`Keynote Speaker, Pennsylvania ASM
`2007
`Distinguished lecture, CDC, Atlanta
`2007
`OKU Distinguished Lecture, NYU College of Dentistry
`2007
`Fellow, New York Academy of Sciences
`2006
`Lloyd Harris Lecturer, U. of Oklahoma
`2006
`G.F. Heinrich keynote lecture, Lang Center, NY Hospital
`2006
`Division M Keynote Address, ASM
`2006
`Chair, NY Academy of Sciences, Microbiology Section
`2006
`COBRE Visiting Scholar, U. Hawaii
`2005
`Keynote address, Southern California ASM
`2004
`McLaughlin Lecturer, University of Texas, Galveston
`2004
`ASM Lecturer, American Society of Virology, Montreal
`2004
`Ellison Medical Foundation Lecture (Wind River Conference, CO)
`2003
`State of the Art Lecture, Am. Society of Virology, Davis, CA
`2003
`Chair, Gordon Conference, Chemical and Biological Terrorism Defense
`2003
`Invited speaker, ASM Biodefense Conference, Baltimore, MD
`2003
`Invited speaker, Banbury meeting on Bacteriophage Biology, CSH, NY
`2002
`Invited speaker, Boston University, Boston, MA
`2002
`Cover article - Nature, Aug. 22. “Defense against Anthrax”
`2002
`Keynote address, International Organization for Mycoplasmology
`2002
`Guest speaker, Swiss Society of Intensive Medicine
`2001
`Keynote address, Joint German Conference for Microbiology
`2000
`Keynote address, Japanese Lancefield Society Annual Meeting
`1999
`John H. Hanks Memorial Lecture, Johns Hopkins School of Public Health
`1999
`Pfizer Lectureship (U. Pittsburgh)
`1999
`1997 - 2007 MERIT Award, National Institutes of Health
`1996 - 1997 Foundation Lecturer, American Academy for Microbiology
`1996
`Keynote address, International Lancefield Society, Paris
`1995
`Invited speaker, Institut Pasteur Symposia, "The Year of Louis Pasteur"
`1994 - Pres Fellow, American Academy for Microbiology
`1994 - 1995 Chairman, Div. B (Microbial Pathogenesis), Am. Society for Microbiology
`1992
`McLaughlin Lecturer, University of Texas, Galveston
`Burroughs Wellcome Visiting Professor, (University of Arizona)
`1992
`1987 - 1997 MERIT Award, National Institutes of Health
`1987
`Invited speaker, Institut Pasteur Centennial
`1987
`Shipley Lecturer, Harvard Medical School
`1986 - 1987 President, Lancefield Society
`1980
`Alumni Achievement Award, Wagner College
`1977 - 1982 Research Career Development Award, National Institutes of Health
`1973 - 1977 Senior Investigator, New York Heart Association
`1971 - 1973 Helen Hay Whitney Foundation Fellowship
`1970
`NYU Founders Day Award for outstanding scholarship (PhD)
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`Professional Activities (selected):
`2019 – Pres. Scientific Advisory Board Lumen Biosciences, Inc.
`2016 – Pres. Scientific Advisory Board, Bioharmony Therapeutics Inc.
`2012 – 2018 Chairman, Scientific Advisory Board, Avacyn Corp
`2012 - 2018 Associate Editor, Microbiology Spectrum, an ASM publication
`2010 – 2019 Scientific Advisory Board, ContraFect Corp.
`2009 – 2017 ASM Press Books Committee
`1994 – Pres. Board of Scientific Advisors and Trustee, Trudeau Institute
`1992 – Pres. Advisory Editor, Trends in Microbiology
`1990 – Pres. Advisory Editor, Journal of Experimental Medicine
`2015 – 2018 Scientific Advisory Board, Symbiotic Health Inc.
`2008 – 2012 Advisory Board: The Center for Structural Genomics of Infectious Diseases
`2009 - 2010 Advisory Board: DTRA (Defense Threat Reduction Agency)
`2004 - 2008 Scientific Advisory Board, Great Lakes Regional Center of Excellence
`2002 - 2010 Chairman, Scientific Advisory Board, Enzybiotics, LLC
`1999 - 2019 Microbiology Advisory Board, New York Academy of Sciences
`1986 - 1996 Advisory Board, New York Hall of Science
`2000 - 2003 Awards Advisory Board, American Society for Microbiology
`1996 - 2002 Scientific Advisory Board, SIGA Technologies
`1999 - 2002 Chairman, Institutional Review Board (IRB), Rockefeller University
`1996 - 2000 Advisory Board, Defense Advanced Research Projects Agency (DARPA)
`1996 - 2001 Chief Scientific Advisor, SIGA Pharmaceuticals
`1989 - 1999 Editor-in-Chief, Infection and Immunity
`1984 - 1998 Co-Director, Biotechnology Facility at the Rockefeller University
`1995 - 1997 Member, Scientific Advisory Board, Spectral Diagnostics
`1993 - 1995 Chairman, Scientific Advisory Board, M6 Pharmaceuticals
`1988 - 1989 Assistant Editor, Journal of Experimental Medicine
`1980 - 1985 Section Editor, Journal of Immunology
`1978 - 1983 NIAID Bacteriology and Mycology Study Section (BM2)
`1978 - 1989 Editorial Board, Infection and Immunity
`1978 - 1980 Editorial Board, Journal of Immunology
`
`Companies: Scientific Founder: M6 Pharmaceuticals, SIGA Technologies, Astoria
`Biologica Inc.
`
`Patents:
` US Patent No.
`
`
`
`
`
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`
`
`# 4,784,948
`
` 1. Production of streptococcal M protein immunogens
`
`# 5,352,588
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` 2. Streptococcal immunoglobulin A binding protein
`
`# 5,556,944
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` 3. Immunoglobulin binding protein ML2.2
`
`# 5,587,288
` 4. Regulation of exoproteins in Staphylococcus aureus
`
`
` 5. Method for exposing group A streptococcal antigens and an improved
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`diagnostic test for the identification of group A streptococci
`# 5,604,109
` 6. Polypeptide of a hybrid surface protein by bacteria
`
`
`# 5,616,686
` 7. Process, apparatus and reagents for isolating cellular components
`# 5,634,767
` (Commercialized as “Fast-prep” RNA/DNA isolation system by Q-biogene)
` 8. Gene for serum opacity factor
`
`
`
`
`
`# 5,707,822
` 9. Delivery and expression of a hybrid surface protein by bacteria
`# 5,786,205
`10. Use of Gram-positive bacteria to express recombinant proteins
`# 5,821,088
`11. Production of streptococcal M protein
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`
`
`
`# 5,840,314
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`Page 3
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`# 5,910,441
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`# 7,402,309
`# 7,569,223
`# 7,582,729
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`# 7,582,281
`# 7,604,975
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`# 7,638,600
`# 8,105,585
`# 8,759,384
`# 9,404,922
`# 9,914,916
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`EP2699689A1
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`EP2699253A2
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`US20190352377A1
`Patent Filed 2019
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`12. Fibronectin/fibrinogen binding protein of group A streptococci
`13. Method for screening inhibitors of the enzyme which cleaves the
`# 5,968,763
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`anchor of surface proteins from Gram-positive bacteria
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`# 5,976,792
`14. Regulation of exoprotein in Staphylococcus aureus II
`
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`# 5,985,654
`15. Recombinant poxvirus and streptococcal M protein vaccine
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`16. Use of bacterial phage associated lysing enzymes for the prophylactic
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`and therapeutic treatment of various illnesses
`
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`# 6,056,954
`17. Plasmin binding protein and therapeutic use thereof
`
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`# 6,190,659
`18. Composition incorporating bacterial phage associated lysing enzymes
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`for treating dermatological infections
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`
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`# 6,277,399
`19. Receptor for Mycobacterium leprae and methods of use thereof
`# 6,331,405
`20. Receptor for Mycobacterium leprae and methods of use thereof
`# 6,331,405
`21. Fibronectin/fibrinogen binding protein of group A streptococci
`# 6,355,477
`22. Synthetic peptides from streptococcal M protein and vaccines prepared
`
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`therefrom
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`
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`# 6,602,907
`23. C1 bacteriophage lytic system
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`# 6,608,187
`24. Phage-associated lytic enzymes for the treatment of Bacillus anthracis
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`and related conditions
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`25. Phage associated lytic enzymes for treatment of pneumonia
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`26. Nucleic acid and polypeptides of C1 bacteriophage and uses thereof
`27. Bacteriophage lysins for Enterococcus faecalis,
`
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`Enterococcus faecium and other bacteria
`
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`28. Glycosylated LPXTGases and uses thereof
`29. Lytic enzymes and spore surface antigen for detection and
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`treatment of Bacillus anthracis bacteria and spores
`30. PlyGBS mutant lysin
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`31. Oxo-Imidazolyl Compounds
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`32. Anthrax diagnostic
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`33. Dimeric bacteriophage lysins
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`33. Streptococcus bacteriophage lysins for treatment of gram
`positive bacteria in companion animals and livestock
`34. Streptococcus bacteriophage lysins for detection
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`and treatment of gram-positive bacteria
`35. Chimeric antibodies comprising binding domains of phage lysins,
`bacterial autolysins, bacteriocins, and phage tail or tail fibers
`36. Recombinant Pseudomonas aeruginosa lysins
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`
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`Societies: American Society for Microbiology, New York Academy of Sciences
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`Contributions to Science
`
`1. The coiled coil structure of streptococcal M protein: M protein is a major virulence
`determinant for S. pyogenes. Despite the fact that this molecule is used to classify streptococci
`into nearly 150 different M types, nothing was known about its structure or conformation. We were
`the first to clone and then sequence the M protein making it the first surface protein on gram-
`positive to be cloned and sequenced, making the M protein the architypical molecule for surface
`proteins on gram-positive organisms. This information verified our previous structurel studied
`indicating that it is a coiled coil molecule that extended 600 nm from the surface of the streptoccus.
` Subsequent sequence data showed that the N-terminal region was the type-specific portion of the
`molecule and the C-terminal half was conserved among the many M proteins that are known. This
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`latter information allowed for strains to be typed genetically based on the variability of the N-
`terminal sequence rather than the cumbersom and expensive serological typing scheme. All this
`information about the M molecule had significant implications in vaccine development as well as
`streptococcal evolution.
`
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`Phillips, G.N., P.F. Flicker, C. Cohen, B.N. Manjula, and V.A. Fischetti. 1981.
`Streptococcal M protein: alpha-helical coiled-coil structure and arrangement on the cell
`surface. Proc. Nat. Acad. Sci. USA. 78:4689-4693.
`Scott, J.R., V.A. Fischetti. 1983. Expression of streptococcal M protein in E. coli. Science,
`221:758-760.
`
`Hollingshead, S., V.A. Fischetti, and J.R. Scott. 1985. The complete nucleotide sequence of
`the streptococcal M6 protein: Repetitive structure and membrane anchor. J. Biol Chem.
`261:1677-1686.
`
`Bessen, D.B. and V.A. Fischetti. 1988. Influence of Intranasal immunization with synthetic
`peptides corresponding to conserved epitopes of M protein on mucosal colonization by
`streptococci. Infect. Immun. 56:2666-2672.
`
`
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`2. Surface protein anchoring in Gram-positive pathogens. Surface proteins on bacteria
`particularly gram-positives are important in survival and pathogenesis, however how these
`molecues are translocated and anchored on the cell surface was not known. During our studies of
`the M protein sequence and as other surface proteins on gram-positives were reported, we
`discovered that nearly all these proteins had a common C-terminal region. We identified a motif
`(LPXTG) that was comon among all these proteins and we proved that this motif was an anchoring
`signal for surface proteins on gram-positive bacteria. This information is now critical for the
`development of anti-infectives and vaccines. Also, by searching the bacterial sequece database
`for molecules with an LPXTG motif close to their C-terminii, the surface location of the molecules in
`the bacterial cell can be predicted. This finding lead to the identification of sortase, the
`transpeptidase responsible for the anchoring process. Inhibition of sortase activity by a small
`molecule can render the orgnism non-virulent and easily cleared by the immune system.
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`Fischetti, V.A., V. Pancholi, and O. Schneewind. 1990. Conservation of a hexapeptide
`sequence in the anchor region of the surface proteins of gram-positive cocci. Mol.
`Microbiol.4:1603-1605
`Schneewind, O., P. Model and V.A. Fischetti. 1992. Sorting of protein A to the
`staphylococcal cell wall. Cell. 70:1-20
`Raz, A. & V. A. Fischetti, (2008) Sortase A localizes to distinct foci on the Streptococcus
`pyogenes membrane. Proc. Nat. Acad. Sci. USA 105: 18549-18554. PMC2587614
`
`
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`3. Identification of biologically active surface proteins on S. pyogenes. Other than M protein,
`not much was known about the surface proteins on S. pyogenes that may be important in their
`pathogenesis. We systematically identified several important molecules that could play a role in
`their pathogenesis and the antiphagocytic activity of the M protein. An important group of
`molecules were five contiguous glycolytic enzymes that are normally found in the cytoplasm but
`are located on the cell surface in a complex with the ability to produce ATP. Many of these same
`molecules are located on other pathogens such as S. aureus, S. pneumoniae, Candida and
`Trypanosomes and reported to be associated with autoimmune diseases.
`
`
`Horstmann, R.D., J. Sievertsen, J. Knoblock and V.A. Fischetti. 1988. Antiphagocytic
`activity of streptococcal M protein: Selective binding of complement control protein Factor H.
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`Proc. Nat. Acad. Sci. USA. 85:1657-1661. PMC279833
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`Pancholi, V., and V.A. Fischetti. 1992. A major surface molecule on group A streptococci is a
`glyceraldehyde-3-phosphate
`dehydrogenase
`with
`multiple
`binding
`activity.
`J.Exp.Med.176:415-426. PMC2119316
`Rakonjac, J.V., J.C. Robbins, and V.A. Fischetti. 1995. DNA sequence of the serum opacity
`factor of class II group A streptococci: Identification of a fibronectin binding repeat domain.
`Infect.Immun. 63:622-631. PMC173041
`
`Pancholi, V. and V.A. Fischetti. 1998. alpha-Enolase, a novel strong plasmin(ogen) binding
`protein on the surface of pathogenic streptococci. J. Biol. Chem. 273:14503-14515.
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`4. Role of bacteriophage in disease and bacterial survival. Bacteriophages are prevalent in
`the environment and from bacterial genome sequence, it appears that they are also common
`inhabitants of bacteria. However, while phage carry virulence determinants on their genomes,
`their role in pathogenesis was poorly understood. For the first time we showed that lysogenic
`bacteriophage are activated in vivo in the presence of a small molecule found in saliva. This
`implies that lysogenic phage could sense their environment and mobilize themselves or molecules
`for their survival. This is clearly seen in B. anthracis, where we show that when vegetative
`organisms enter the soil, they become lysogenized by soil phage, converting them to free living
`organisms able to survive in the soil. We also found that while lysogeny is believed to be phage
`incorporation in the bacterial host DNA, there is a prevalence or plasmidial phage in the cytoplasm
`of pathogens (particularly B. anthracis and S. aureus) that contain virulence determinants that
`would be missed during normal bacterial genome sequencing. Thus, we have identified a potential
`reservoir of virulence genes that have not been previously considered.
`
`
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`Broudy, T., and V.A. Fischetti, 2003. In vivo lysogenic conversion of Tox- S. pyogenes to
`Tox+ with lysogenic streptococci or free phage. Infect Immun. 71:3782-3786. PMC161974
`
`Schuch, R., V.A. Fischetti. 2006. Detailed genomic analysis of the gamma and W1 phage
`infecting B. anthracis: Implications for phage in environmental fitness and antibiotic resistance.
`J. Bacteriol 188: 3037-3051. PMC1446989
`
`Schuch, R. and VA Fischetti. 2009. The secret life of the anthrax agent B. anthracis. PLoS-
`One 4(8): e6532. doi:10.1371. PMC2716549
`
`Utter, B., R. Schuch, B.Y. Winer, K. Verratti, K. Bishop-Lilly, S. Sozhamannan, and V.A.
`Fischetti. 2014. Beyond the chromosome: Staphylococcus aureus extrachromosomal DNA
`identifies several unique plasmidial bacteriophages carrying virulence genes. PLoS-One, June
`25;9(6):e100502. PMC4070920
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`
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`5. Lysins as novel therapeutics. Given the increase in antibiotic resistance by pathogenic
`bacteria, new methods must be devised to control these pathogens. My laboratory was involved in
`streptococcal vaccine development (see above) and early in my carreer I had characterized a
`phage lysin from a streptococcal phage and used that lysin to extract surface proteins on S.
`pyogenes. Given the problems with antibiotic resistance, I performed an experiment to determine
`if the phage lysin could decolonize S. pyogenes from the throats of mice. Mice colonized with S.
`pyogenes and treated with one dose of lysin orally, were decolonized of the streptococci. This was
`the first publication describing the therapeutic effects of phage lysins. During the ensuing 18
`years, we developed phage lysins against all of the major gram-positive pathogens and we now
`have lysins against gram-negative pathogens. A staphylococcal-specific lysin that we developed is
`currently in phase 3 human clinical trials and if successful, this could be the turning point for the
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`widespread therapeutic use of lysins.
`
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`Nelson, D., L. Loomis, and V.A. Fischetti. 2001. Prevention and elimination of upper
`respiratory colonization of mice by group A streptococci using a bacteriophage lytic enzyme.
`Proc Nat Acad Sci USA. 98:4107-4112. PMC31187
`
`Loeffler, J., D. Nelson, and V.A. Fischetti. 2001. Rapid killing in of S. pneumoniae with a
`bacteriophage cell wall hydrolase. Science. 294:2170-2172.
`
`Schuch, R., D. Nelson and V.A. Fischetti. 2002. A bacteriolytic agent that detect and kills
`Bacillus anthracis. Nature. 418: 884–889.
`Gilmer, D.B, J.E. Schmitz, C.W. Euler, and V.A. Fischetti. 2013. Novel Bacteriophage Lysin
`with Broad Lytic Activity Protects Against Mixed Infection by Streptococcus pyogenes and
`Methicillin-Resistant Staphylococcus aureus. Antimicrob Agents Chemother, 9 April 2013,
`doi: 10.1128/ AAC.02526-12. PMC3716137.
`
`6. Lysibodies: Engineered immunoglobulins to control S. aureus. The cell wall of Gram-
`positive bacteria contains abundant surface-exposed carbohydrate structures that are highly
`conserved. While these properties make surface carbohydrates ideal targets for immunotherapy,
`carbohydrates elicit a notoriously poor immune response. We have been successful in engineering
`a hybrid IgG molecule called a “Lysibody” that is directed to carbohydrate epitopes in the bacterial
`cell wall (REF). Lysibodies are engineered molecules combining in a single molecule a high-
`affinity carbohydrate-binding domain from enzymes of bacterial or bacteriophage origin, and the Fc
`effector portion of human IgG1, forming a hybrid immunoglobulin with all the effector functions of
`normal human IgG. Currently, there are no vaccines or immunoglobulins against S. aureus since
`most antibodies were directed to protein targets that can vary among different strains, and their
`expression is also variable. A lysibody directed against methicillin resistant Staphylococcus aureus
`(MRSA) is currently in pre-clinical development to be used as prophylaxis in pre-surgical and
`dialysis patients and neonates to prevent MRSA and other staphylococcal infections.
`
`Raz, A., A. Serrano ,C. Lawson, M. Thaker, T. Alston, S. Bournazos J.V. Ravetch, V.A.
`
`Fischetti. 2017. Lysibodies – engineered opsonic IgG chimeras to Staphylococcus aureus wall
`carbohydrates. Proc. Nat. Acad. Sci. April 2017.
`
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`Raz, A, A. Serrano, M. Thaker, T. Alston and V.A. Fischetti. 2018. Lysostaphin and lysK
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`lysibodies lead to effective opsonization and killing of methicillin resistant Staphylococcus aureus.
`Submitted.
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`BIBLIOGRAPHY
`
`Vincent A. Fischetti, Ph.D.
`
`
`WEB SITE: http://www.rockefeller.edu/vaf
`
`ORIGINAL ARTICLES and REVIEWS: Most significant in italics
`
`1. Fischetti, V.A., B. Barron, and J.B. Zabriskie. 1968. Studies on streptococcal
`bacteriophage. I. Burst size and intracellular growth of group A and group C streptococcal
`bacteriophages. J. Exp. Med. 127:475.
`
`2. Fischetti, V.A., and J.B. Zabriskie. 1968. Studies on streptococcal bacteriophage. II.
`Adsorption studies on group A and group C streptococcal bacteriophages. J. Exp. Med.
`127:489.
`
`3. Barron, B., V.A. Fischetti, and J.B. Zabriskie. 1970. Studies of bacteriophage kinetics in
`multicellular systems: a statistical model for the estimation of burst size per cell in streptococci.
`J. Applied Bact. 33:436.
`
`4. Ellis, R.J., C.W. Lillehei, V.A. Fischetti, and J.B. Zabriskie. 1970. Heart-reactive antibody:
`a measure of heart rejection in human heart transplants. Circulation, XLI and XLII,
`Supplement II. 81-97.
`
`5. Fischetti, V.A., E.C. Gotschlich, and A.W. Bernheimer. 1971. Purification and physical
`properties of group C streptococcal phage-associated lysin. J. Exp. Med. 133:1105.
`
`6. Zabriskie, J.B., V. Utermohlen, S.E. Read, and V. Fischetti. 1973. Streptococcus-related
`glomerulonephritis. Kidney Int. 3:100.
`
`7. Read, S.E., V.A. Fischetti, V. Utermohlen, R.E. Falk, and J.B. Zabriskie. 1974. Cellular
`reactivity studies to streptococcal antigens. Migration inhibition studies in patients with
`streptococcal infections and rheumatic fever. J. Clin. Invest. 54:439.
`
`8. Fischetti, V.A., G. Siviglia, J.B. Zabriskie, and E.C. Gotschlich. 1976. Radioiodination of
`non-ionic detergents of the alkyl-phenol class: Triton X-100. Anal. Biochem. 73:65.
`
`9. Fischetti, V.A., E.C. Gotschlich, G. Siviglia, and J.B. Zabriskie. 1976. Streptococcal
`M-proteins extracted by non-ionic detergent. I. Properties of the antiphagocytic and type-specific
`molecules. J. Exp. Med. 144:32.
`
`10. Read, S.E., H. Reid, T. Poon-King, V.A. Fischetti, J.B. Zabriskie, and F.T. Rapaport.
`1977. HLA and predisposition to the non-suppurative sequelae of group A streptococcal
`infection. Transplantation Proc. IX (1):543-546.
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`1977
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`1980
`
`1981
`
`1983
`
`11. Fischetti, V.A. 1977. Streptococcal M protein extracted by non-ionic detergent. II. Analysis
`of the antibody response to the multiple antigenic determinants of the M protein molecule. J.
`Exp. Med. 146:1108.
`
`12. Fischetti, V.A., E.C. Gotschlich, G. Siviglia, and J.B. Zabriskie.1977. Streptococcal M
`protein: an antiphagocytic molecule assembled on the cell wall. J. Infect. Dis. 136: S222-S233.
`
`13. Fischetti, V.A. 1978. Streptococcal M protein extracted by non-ionic detergent. III.
`Correlation between immunological cross-reactions and structural similarities with implications
`for antiphagocytosis. J. Exp. Med. 47:1771.
`
`14. Villarreal, H., Jr., V.A. Fischetti, I. van de Rijn, and J.B. Zabriskie. 1979. The
`occurrence of a protein in the extracellular products of streptococci isolated from patients with
`acute glomerulonephritis. J. Exp. Med. 149:459.
`
`15. Hosein, B., M. McCarty, and V.A. Fischetti. 1979. Amino acid sequence and
`physicochemical similarities between streptococcal M-protein and mammalian tropomyosin.
`Proc. Natl. Acad. Sci. USA 76:3765.
`
`16. Manjula, B.N., and V.A. Fischetti. 1980. Studies on group A streptococcal M-proteins.
`Purification of type 5 M-protein and comparison of its amino terminal sequence with two
`immunologically unrelated M-protein molecules. J. Immunol. 124:261-267.
`
`17. Manjula, B.N., and V.A. Fischetti. 1980. A tropomyosin-like seven residue periodicity in
`three
`immunologically distinct streptococcal M-proteins and
`its
`implications
`for
`the
`antiphagocytic property of the molecule. J. Exp. Med. 151:695-708.
`
`18. van de Rijn, I. and V.A. Fischetti. 1981. Immunochemical analysis of intact M protein
`secreted from cell wall-less streptococci. Infect. Immun. 32:86-91.
`
`19. Phillips, G.N., P.F. Flicker, C. Cohen, B.N. Manjula, and V.A. Fischetti. 1981.
`Streptococcal M protein: alpha-helical coiled-coil structure and arrangement on the cell surface.
`Proc. Nat. Acad. Sci. USA. 78:4689-4693.
`
`20. Fischetti, V.A., 1983. Requirements for opsonic activity of human IgG directed to type 6
`group A streptococci: Net basic charge and intact Fc region. J. Immunol. 130:896-902.
`
`21. Schutzer, S.E., V.A. Fischetti, and J.B. Zabriskie. 1983. Toxic shock syndrome and
`lysogeny in Staphylococcus aureus. Science. 120:316-318.
`
`22. Ohkuni, H., J. Friedman, I. Van de Rijn, V.A. Fischetti, T. Poon-King and J.B. Zabriskie.
`1983. Immunological studies on post-streptococcal sequelae: I. Serological studies with an
`extracellular protein associated with nephritogenic streptococci. Clin. Exp. Immun. 54:185-193.
`
`23. Manjula, B.N., S.M. Mische and V.A. Fischetti. 1983. Primary structure of streptococcal
`pep M5 protein: Absence of extensive sequence repeats. Proc. Nat. Acad. Sci. USA.
`80:5475-5479.
`
`24. Acharya, A.S., A. Di Donato, B.N. Manjula, V.A. Fischetti, and J.M. Manning. 1983.
`Influence of trifluoracetic acid on retention times of histidine-containing tryptic peptides in
`reverse phase HPLC. Int. J. Peptide Protein Res. 22:78-82.
`
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`
`
`Original articles,
`
`
`cont.
`
`25. Scott, J.R., V.A. Fischetti. 1983. Expression of streptococcal M protein in E. coli. Science,
`221:758-760.
`1984
`26. Manjula, B.N., A.S Acharya, S.M. Mische, T. Fairwell and V.A. Fischetti. 1984. Complete
`amino acid sequence of a biologically active 197-residue fragment of M protein isolated from
`type 5 streptococci. J. Biol. Chem. 259:3686-3693.
`
`27. Fischetti, V.A., K.F. Jones, B.N. Manjula, and J.R. Scott. 1984. Streptococcal M protein
`expressed in Escherichia coli: Purification, characterization, and comparison with streptococcal
`derived M protein. J. Exp. Med. 159:1083-1095.
`
`28. Friedman, J., I. van de Rijn, H. Ohkuni, V.A. Fischetti, and J.B. Zabriskie. 1984.
`Immunological studies of post-streptococcal sequelae: evidence for presence of streptococcal
`antigens in circulating immune complexes. J. Clin Invest. 74:1027-1034.
`
`1985
`
`1986
`
`29. Scott, J.R., W.M. Pulliam, S.K. Hollingshead and V.A. Fischetti. 1985. Relationship of M
`protein genes in group A streptococci. Proc. Nat. Acad. Sci. USA. 82:1822-1826.
`
`30. Manjula, B.N., B. Trus, and V.A. Fischetti. 1985. The presence of two distinct regions in
`the coiled-coil structure of streptococcal pep M5 protein: Relation to mammalian coiled-coil
`its biological properties. Proc. Nat. Acad. Sci. U.S.A.
`proteins and
`implications
`to
`82:1064-1068.
`
`31. Jones, K.F., B.N. Manjula, K.H. Johnston, S.K. Hollingshead, J.R. Scott and V.A.
`Fischetti. 1985. The location of variable and conserved epitopes among the variable serotypes
`of streptococcal M protein. J. Exp. Med. 161:623-628.
`
`32. Fischetti, V.A., K.F. Jones, and J.R. Scott. 1985. Size variation of the M protein in group A
`streptococci. J. Exp. Med. 161:1384-1401.
`
`33. Manjula, B.N., M. Schmidt, and V.A. Fischetti. 1985. Unimpaired function of human
`phagocytes in the presence of phagocytosis-resistant group A streptococci. Infect. Immun.
`50:610-613.
`
`34. Chalovich, J.M. and V.A. Fischetti. 1985. Crosslinking of actin filaments and inhibition of
`S-1 ATPase activity by streptococcal M6 protein. Arch. Biochem. Biophys. 245:37-43.
`
`35. Manjula, B.N., A.S. Acharya, T. Fairwell, and V.A. Fischetti. 1985. Antigenic domains of
`the streptococcal Pep M5 protein: Localization of epitopes cross- reactive with type 6 M protein
`and identification of a hypervariable region of the M molecule. J. Exp. Med. 163:129-138.
`
`36. Hollingshead, S., V.A. Fischetti, and J.R. Scott. 1985. The complete nucleotide sequence
`of the streptococcal M6 protein: Repetitive structure and membrane anchor. J. Biol Chem.
`261:1677-1686.
`
`37. Scott, J.R., S.K. Hollingshead and V.A. Fischetti. 1986. Homologous regions within M
`protein genes in group A streptococci. Infect. Immun. 52:609-612.
`
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`Original articles,
`
`
`cont.
`38. Fischetti, V.A., M. Jarymowycz, K.F. Jones, S. Hollingshead, and J.R. Scott. 1986.
`Streptococcal M protein size mutants occur at high frequency within a single strain. J. Exp.
`Med. 164:971-980.
`
`39. Jones, K.F., S.A. Kahn, B.W. Erickson, S.K. Hollingshead, J.R. Scott and V.A.
`Fischetti. 1986. Immunochemical localization and amino acid sequence of cross-reactive
`epitopes within the group A streptococcal M6 protein. J. Exp. Med. 164:1226-1238.
`
`40. Manjula, B.N. and V.A. Fischetti. 1986. Sequence homology of group A streptococcal
`PepM5 protein with other coiled-coil proteins. Biochem. Biophys. Res. Comm. 140:684-690.
`
`41. Read, S.E., H.F.M. Reid, V.A. Fischetti, T. Poon-King, R. Ramkissoon, M. McDowell
`and J.B. Zabriskie. 1986. Serial studies on the cellular immune response to streptococcal
`antigens in acute and convalescent rheumatic fever patients in Trinidad. J. Clin. Immunol.
`6:1-9.
`
`42. Scott, J.R., P.C. Guenthner, L.M. Malone, and V.A. Fischetti. 1986 Conversion of an M-
`group A streptococcus to M+ by transfer of a plasmid containing an M6 gene. J. Exp. Med.
`164:1641-1651.
`
`1987
`
`43. Jones, K.F. and V.A. Fischetti. 1987. Biological and immunological identity of M protein on
`group G streptococci with M protein on group A streptococci. Infect. Immun. 55:502-506.
`
`44. Mische, S.M., B.N. Manjula, and V.A. Fischetti. 1987. Relation of Streptococcal M protein
`with human and rabbit tropomyosin: The complete amino acid sequence of human cardiac
`alpha tropomyosin, a highly conserved contractile protein. Biochem. Biophys. Res. Comm.
`142:813-818.
`
`45. Hollingshead, S.K., V.A. Fischetti, and J.R. Scott. 1987. Size variation in group A
`streptococcal M protein is generated by homologous recombination between intragenic repeats.
`Molec. Gen.Genet. 207:196-203.
`
`46. Hollingshead, S.K., V.A. Fischetti, and J.R. Scott. 1987. A highly conserved region
`present in transcripts encoding heterologous M proteins of group A streptococci. Infec