Richard W Compans, PhD
Emory Vaccine Center
Department of Microbiology and Immunology, Emory University School of Medicine
Emory Center for AIDS Research
Dr. Compans is a Professor in (and former Chair of) the Department of Microbiology and Immunology in the Emory University School of Medicine and is the Scientific Director of the Influenza Pathogenesis & Immunology Research Center (IPIRC). Before coming to Emory in 1992, he was a professor in the microbiology department of the University of Alabama at Birmingham. Dr. Compans received his Ph.D. from the Rockefeller University.
Richard W. Compans, Ph.D is Professor in the Department of Microbiology and Immunology in Emory University School of Medicine, and Scientific Director of the Emory/UGA Center of Excellence for Influenza Research and Surveillance.. He received his Ph.D. from Rockefeller University, where he studied the structure and assembly of parainfluenza viruses with Dr. Purnell W. Choppin, and carried out postdoctoral research on influenza virus with Dr. Frank Fenner at the Australia National University. Early studies on influenza virus by Dr. Compans and colleagues included characterization of the virion polypeptides, analysis of their organization in the virion , their biosynthesis and intracellular transport; determining the structure of the influenza helical nucleocapsid, demonstration that the influenza viral lipids are organized in a bilayer structure, and defining the function of the viral neuraminidase. Extensive studies were carried out on the use of influenza virus as a system for investigating the determinants of protein sorting and polarized virus release in epithelial cells. More recent studies have shown that the M1 and M2 proteins are important determinants of the morphology of the virion (spherical vs. filamentous).
Extensive studies have also been carried out by Dr. Compans’ laboratory on development of novel vaccines and improved approaches to vaccination. Virus-like particles (VLPs) have been developed as vaccine antigens for HIV, Ebola, influenza and respiratory syncytial viruses. The VLPs are more effective at inducing neutralizing antibody responses than purified viral proteins because they are particulate antigens with repetitive arrangements of viral proteins on their surfaces. In studies with HIV VLPs, we found that Env proteins with a modified cytoplasmic domain exhibited the highest levels of incorporation into VLPs and induced the highest titers of anti-Env immune responses. Sera from guinea pigs immunized by these VLPs with high Env content, and containing a CT trimerization sequence, had increased neutralization activity and antibody avidity. A cross-clade prime-boost regimen with DNA priming and boosting with VLPs further enhanced these immune responses. The modified VLPs demonstrate improved potential as HIV-1 vaccine antigens.In collaboration with Georgia Tech, we also have observed that delivery of viral antigens to the skin using vaccine-coated microneedles induces higher titers of protective antibodies and longer duration of immunity than conventional intramuscular immunization.
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