Christopher C. Broder


Department of Primary Appointment:
School of Medicine
Microbiology and Immunology
Professor and Chair
Location: Uniformed Services University of the Health Sciences, Bethesda, MD
Research Interests:
Virology; emerging viruses, virus-host cell interactions, vaccines and therapeutics, viral serological surveillance
Basic Biology of Bacterial, Viral, or Parasite Diseases
Office Phone


1983 B.S., Biological Sciences, with honors. Florida Institute of Technology, Melbourne, Florida.
1985 M.S., Molecular Biology, Florida Institute of Technology, Melbourne, Florida.
1989 Ph.D., Microbiology and Immunology. College of Medicine, University of Florida, Gainesville, Florida.


Christopher C. Broder received his B.S. (1983) and M.S. (1985) degrees from the Florida Institute of Technology, Melbourne. He earned his Ph.D. from the University of Florida, Gainesville (1989) establishing a molecular-pathogenic model for the flesh-eating Group A streptococci. He began his postdoctoral studies in 1989 as a National Research Council Research Associate in the Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, focusing on HIV-1 host cell entry and infection. He joined the faculty of the Department of Microbiology and Immunology at Uniformed Services University (USU) as Assistant Professor in 1996 and rose through the ranks to become a full Professor in 2005. His laboratory has focused on virus-host cell interactions with an emphasis on virus receptor discovery, virus entry and virus-mediated membrane fusion, vaccines and antibody therapeutics development. Research areas include HIV-1 and emerging zoonotic viruses including Nipah virus and Hendra virus; Ebola and Marburg viruses, and bat lyssavirus. His major collaborative research contributions include the discoveries of the CXCR4 and the CCR5 HIV-1 coreceptors (1996-Breakthrough of the Year, Science magazine and the AAAS Newcomb Cleveland Prize 1997); the development of the first oligomeric, HIV-1 soluble gp140 glycoprotein vaccine candidate; discovery of the host cell receptor proteins (ephrin ligands) used by Nipah virus and Hendra virus; development of the Hendra/Nipah soluble-G glycoprotein subunit vaccine; one formulation known as Equivac® HeV (Zoetis, Inc.), the first commercialized vaccine against a BSL-4 agent. Clinical development of the soluble G subunit vaccine for Nipah and Hendra for human-use is underway by Profectus Biosciences, Inc., and partners, supported by CEPI (The Coalition for Epidemic Preparedness Innovations). Therapeutic antiviral human monoclonal antibodies have also been developed, including the anti-Hendra/Nipah human mAb m102.4 which has been used by emergency protocol in 13 people in Australia and one in the U.S. because of significant risk of Hendra or Nipah virus infection. The m102.4 antibody has completed a Phase I clinical trial in Australia, and has recently been supplied to Government of India and included in an international Nipah treatment protocol sponsored by the Indian Council of Medical Research (ICMR) in collaboration with the WHO, NIAID, NIH, USA. Recent honors include the 2013 and 2019 Federal Laboratory Consortium (FLC) Awards for Excellence in Technology Transfer; the CSIRO Chairman’s Medal for 2013, (Australia's national science agency); the 2014 Cinda Helke Award for Excellence in Graduate Student Advocacy; the 2016 James J. Leonard Award for Excellence in Translational/Clinical Research; and the inaugural, 2020 Federal Laboratory Consortium (FLC) Impact Award. He has mentored 13 graduate students and 12 postdoctoral scientists; coauthored more than 180 scientific articles and book chapters cited more 20,000 times; serves on the editorial board of five journals, and is an inventor on 19 US and foreign patents. He served as Director of the Emerging Infectious Diseases Graduate Program at USU from 2006-2018, and is currently Professor and Chair of the Department of Microbiology and Immunology, USU.

Representative publications, projects, and/or deployments

Viral serological surveillance in wildlife and livestock:

Li, Y, Wang, J, Hickey, AC, Zhang, Y, Li, Y, Wu, Y., Zhang, H, Yuan, J, Han, Z, McEachern, J, Broder, CC, Wang, LF, Shi, Z. Antibodies to Nipah or Nipah-like viruses in bats, China. Emerg Infect Dis. 14(12):1974-6 2008.

Chowdhury S, Khan SU, Crameri G, Epstein JH, Broder CC, Islam A, Peel AJ, Barr J, Daszak P, Wang LF, Luby SP. Serological evidence of henipavirus exposure in cattle, goats and pigs in Bangladesh. PLoS Negl Trop Dis. 2014 Nov 20;8(11):e3302. doi: 10.1371/journal.pntd.0003302. 2014 Nov.

Lyssavirus-host cell interactions

:Weir DL, Smith IL, Bossart KN, Wang LF and Broder CC. Host cell infection tropism mediated by Australian bat lyssavirus envelope glycoproteins. Virology, 2013; 444(1-2):21-30. Virology Highlights:

Weir DL, Laing ED, Smith IL, Wang LF, Broder CC. Host cell virus entry mediated by Australian bat lyssavirus G envelope glycoprotein occurs through a clathrin-mediated endocytic pathway that requires actin and Rab5. Virol J. 2014 Feb 27;11(1):40.

Structural studies on viral envelope glycoproteins

:Xu K, Rockx B, Xie Y, DeBuysscher BL, Fusco DL, Zhu Z, Chan YP, Feldmann H, Dimitrov DS, Broder CC, and Nikolov DB. Crystal structure of the Hendra virus attachment G glycoprotein complexed with a potent cross-reactive neutralizing human monoclonal antibody. Plos Pathogens, 2013 Oct;9(10):e1003684.

Xu K, Chan YP, Bradel-Tretheway B, Akyol-Ataman Z, Zhu Y, Dutta S, Yan L, Feng YR, Wang LF, Skiniotis G, Lee B, Zhou ZH, Broder CC*, Aguilar HC* and Nikolov DB*. Crystal structure of the pre-fusion Nipah virus fusion glycoprotein reveals a novel hexamer-of-trimers assembly. PLoS Pathog. 2015 Dec 8;11(12):e1005322. doi: 10.1371/journal.ppat.1005322


Broder, CC, PL Earl, D Long, B Moss, and RW Doms. Antigenic Implications of HIV-1 Envelope Glycoprotein Quaternary Structure: Oligomer-Specific and -Sensitive mAbs. Proc. Natl. Acad. Sci. USA. 91:11699-11703, 1994.

Broder, CC and EA Berger. Fusogenic Selectivity of the Envelope Glycoprotein is a Major Determinant of HIV-1 Tropism for CD4+ T-Cell Lines vs. Macrophages. Proc. Natl. Acad. Sci. USA. 92:9004-08, 1995.

Feng, Y, CC Broder, PE Kennedy, and EA Berger. HIV-1 Entry Cofactor: Functional cDNA Cloning of a Seven-Transmembrane, G Protein-Coupled Receptor. Science. 272:872-877, 1996.

Bonaparte, MI, AS Dimitrov, KN Bossart, G Crameri, BA Mungall, KA Bishop, V Choudhry, DS Dimitrov, LF Wang, BT Eaton, and CC Broder*. Ephrin-B2 Ligand is a Functional Receptor for Hendra Virus and Nipah Virus. Proc Natl Acad Sci U S A. 102(30):10652-7. 2005. (from the cover)

Bossart KN, Rockx B, Feldmann F, Brining D, Scott D, Lacasse R, Geisbert JB, Feng YR, Chan YP, Hickey AC, Broder CC*, Feldmann H, Geisbert TW. A Hendra virus G glycoprotein subunit vaccine protects African green monkeys from Nipah virus challenge. Sci Transl Med. 4(146):146ra107. 2012

Middleton D, Pallister J, Klein R, Feng YR, Haining J, Arkinstall R, Frazer L, Huang JA, Edwards N, Wareing M, Elhay M, Hashmi Z, Bingham J, Yamada M, Johnson D, White J, Foord A, Heine HG, Marsh GA, Broder CC, Wang LF. Hendra virus vaccine, a one health approach to protecting horse, human, and environmental health. Emerg Infect Dis. 2014 Mar;20(3).

Geisbert TW, Mire CE, Geisbert JB, Chan YP, Agans KN, Feldmann F, Fenton KA, Zhu Z, Dimitrov DS, Scott DP, Bossart KN, Feldmann H, Broder CC*. Therapeutic treatment of Nipah virus infection in nonhuman primates with a neutralizing human monoclonal antibody. Sci Transl Med. 2014, 6(242):242ra82.

Laing, ED, Navaratnarajah, CK, Cheliout Da Silva, S, Petzing, SR, Xu, Y, Sterling, SL, Marsh, GA, Wang, LF, Amaya, M, Nikolov, DB, Cattaneo R, Broder, CC*, and Xu, K. Structural and Functional Analyses Reveal Promiscuous and Species-Specific Use of Ephrin Receptors by Cedar Virus. Proc Natl Acad Sci U S A. 2019 Oct 8;116(41):20707-20715.

Dang, HV, Chan, YP, Park, YJ, Snijder, J, Cheliout Da Silva, S, Vu, B, Yan, L, Feng, YR, Rockx, B, Geisbert, TW, Mire, CE, Broder, CC*, and Veesler, D*. A potent cross-neutralizing antibody targeting the fusion glycoprotein inhibits Nipah virus and Hendra virus infection. Nat Struct Mol Biol. 2019; 26:980-7.

Playford EG, Munro T, Mahler SM, Elliott S, Gerometta M, Hoger KL, Jones ML, Griffin P, Lynch KD, Carroll H, El Saadi D, Gilmour ME, Hughes B, Hughes K, Huang E, de Bakker C, Klein R, Scher MG, Smith IL, Wang LF, Lambert SB, Dimitrov DS, Gray PP, Broder CC. Safety, tolerability, pharmacokinetics, and immunogenicity of a human monoclonal antibody targeting the G glycoprotein of henipaviruses in healthy adults: a first-in-human, randomised, controlled, phase 1 study. Lancet Infect Dis. 2020, S1473-3099