John P. Moore, PhD
Professor
Department of Microbiology and Immunology
Weill Medical College of Cornell University
New York, NY

 

Research Topics

• HIV entry into target cells and its inhibition by neutralizing antibodies and specific antiretroviral drugs
• Env-based HIV vaccines
• Entry-inhibitor-based vaginal microbicides

 

Lecture and Writing Topics

• HIV entry and its inhibition
• CCR5 inhibitors and resistance to them
• Env-based vaccines
• ARV-based microbicides

 

Current Professional Summary

Dr Moore is a tenured Professor in the Department of Microbiology and Immunology at Weill Cornell Medical College, where he also conducts basic HIV research. He lectures to PhD and medical students on some areas of HIV-related sciences.

 

Committees and Organizations

• Scientific Advisory Board, UMass CFAR (2000-present)
• Advisory Board Member, Scientific American (2009-present)
• Full Member, CSR Study Section ARR-C (ARR-1) (1997-2001)
• Pediatric AIDS Foundation Grant Review Committee (1999-2004)
• Member, NIAID AIDS Vaccine Research Working Group (2002-2004)

 

Honors and Awards

• Bristol Myers Squibb Infectious Disease Award (2004)
• TAG ‘Research in Action’ Award (2002)
• NIAID MERIT Award (R37) in respect of RO1 AI36082 (1998)
• Elizabeth Glaser Scientist, Pediatric AIDS Foundation (1996)

 

Education

• Cambridge University, BA in Biochemistry (1978)
• Cambridge University, M Phil in Biochemistry (1979)
• Cambridge University, MA in Biochemistry (1981)
• Cambridge University, PhD in Biochemistry (1982)

 

Selected Publications

1. Veazey RS, Klasse PJ, Schader SM, et al. Protection of macaques from vaginal SHIV challenge by vaginally delivered inhibitors of virus-cell fusion. Nature. 2005;438:99-102.
2. Veazey RS, Springer MS, Marx PA, et al. Protection of macaques from vaginal SHIV challenge by an orally delivered CCR5 inhibitor. Nat Med. 2005;11:1293-1294.
3. Veazey RS, Shattock RJ, Pope M, et al. Prevention of virus transmission to macaque monkeys by a vaginally applied monoclonal antibody to HIV-1 gp120. Nat Med. 2003;9:343-346.
4. Trkola A, Kuhmann SE, Strizki JM, et al. HIV-1 escape from a small molecule, CCR5-specific entry inhibitor does not involve CXCR4 use. Proc Natl Acad Sci U S A. 2002;99:395-400.
5. Binley JM, Sanders RW, Clas B, et al. A recombinant human immunodeficiency virus type 1 envelope glycoprotein complex stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits is an antigenic mimic of the trimeric virion-associated structure. J Virol. 2000;74:627-643.
6. Dragic T, Trkola A, Thompson DA, et al. A binding pocket for a small molecule inhibitor of HIV-1 entry within the transmembrane helices of CCR5. Proc Natl Acad Sci U S A. 2000;97:5639-5644.
7. Morris L, Binley JM, Clas BA, et al. HIV-1 antigen-specific and -nonspecific B cell responses are sensitive to combination antiretroviral therapy. J Exp Med. 1998;188:233-245.
8. Moore JP, Sodroski J. Antibody cross-competition analysis of the human immunodeficiency virus type 1 gp120 exterior envelope glycoprotein. J Virol. 1996;70:1863-1872.
9. Dragic T, Litwin V, Allaway GP, et al. HIV-1 entry into CD4+ cells is mediated by the chemokine receptor CC-CKR-5. Nature. 1996;381:667-673.
10. Trkola A, Dragic T, Arthos J, et al. CD4-dependent, antibody-sensitive interactions between HIV-1 and its co-receptor CCR-5. Nature. 1996;384:184-187.
11. Moore JP, Cao Y, Qing L, et al. Primary isolates of human immunodeficiency virus type 1 are relatively resistant to neutralization by monoclonal antibodies to gp120, and their neutralization is not predicted by studies with monomeric gp120. J Virol. 1995;69:101-109.
12. Sattentau QJ, Moore JP. Human immunodeficiency virus type 1 neutralization is determined by epitope exposure on the gp120 oligomer. J Exp Med. 1995;182:185-196.
13. Moore JP, Sattentau QJ, Wyatt R, Sodroski J. Probing the structure of the human immunodeficiency virus surface glycoprotein gp120 with a panel of monoclonal antibodies. J Virol. 1994;68:469-484.
14. Moore JP, Ho DD. Antibodies to discontinuous or conformationally sensitive epitopes on the gp120 glycoprotein of human immunodeficiency virus type 1 are highly prevalent in sera of infected humans. J Virol. 1993;67:863-875.
15. Moore JP, McKeating JA, Weiss RA, Sattentau QJ. Dissociation of gp120 from HIV-1 virions induced by soluble CD4. Science. 1990;250:1139-1142.