HIV Neutralizing Antibodies and Vaccine Antigen Selectively Interact with Phase-Separated Model Membranes

Gregory Hardy
Special Instructions: 
Lunch will be Served!
Friday, October 4, 2013 - 12:30pm
Hudson Hall Room 115 @ Noon, Lunch will be served.
Seminar Contact(s): 
Wes Ross (
Semester & Year: 
Fall 2013

Speaker: Greg Hardy


Evidence suggests that lipid membrane interactions with rare, broadly neutralizing

antibodies (NAbs), 2F5 and 4E10, play a critical role in HIV-1 neutralization. The

objective of this research is to understand how lipid domains contribute to 2F5/4E10

membrane interactions and antigen localization, with the ultimate vision of guiding

immunogen designs. It is well established that the native viral membrane is

heterogeneous, representing a mosaic of lipid rafts and protein clustering. However, the

size, physical properties, and dynamics of these regions are poorly characterized and their

potential roles in HIV-1 neutralization are also unknown. To understand how lipid

domains contribute to 2F5/4E10 membrane interactions, we have engineered biomimetic

supported lipid bilayers (SLBs) and are able to use atomic force microscopy to visualize

membrane domains, antigen clustering, and antibody-membrane interactions.





Greg is a fifth year PhD student in Dr. Zauscher's lab with a B.S. in biomedical

engineering from the University of Rochester. His graduate research is focused on using

biophysical tools applied to protein-membrane interactions in the context of HIV vaccine