Mechanistic and structural studies on amyloid fibrils found in semen that enhance HIV infectivity
Authors
French, Kinsley Claire
ORCID
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Other Contributors
Makhatadze, George I.
Barquera, Blanca L.
GarcÃa, Angel E.
Colón, Wilfredo
Wang, Chunyu
Barquera, Blanca L.
GarcÃa, Angel E.
Colón, Wilfredo
Wang, Chunyu
Issue Date
2014-05
Keywords
Biology
Degree
PhD
Terms of Use
This electronic version is a licensed copy owned by Rensselaer Polytechnic Institute, Troy, NY. Copyright of original work retained by author.
Full Citation
Abstract
Although many amyloid fibrils are involved in neurodegenerative diseases, numerous peptides form amyloid fibrils in semen which increase HIV and other retrovirus infectivity. Interestingly, this effect seems to be limited to the fibrillar state of the peptides since little to no infectivity enhancement is observed when cells are exposed to the non-fibrillar form of the peptides. Since sexual transmission accounts for approximately 80% of new HIV infections and semen markedly enhances HIV infection rates in vitro, semen-derived amyloid fibrils that increase HIV infectivity may be targets for therapeutic development. This study aims to determine the mechanism of fibril formation; the structure of the amyloid fibrils; the interactions that occur between semen-derived amyloid fibrils, HIV, and the cell surface; and the mechanism of fibril-mediated enhancement of viral infectivity. The ultimate goal of these studies is to develop therapeutics capable of ameliorating fibril-mediated enhancement of HIV infectivity.
Description
May 2014
School of Science
School of Science
Department
Dept. of Biological Sciences
Publisher
Rensselaer Polytechnic Institute, Troy, NY
Relationships
Rensselaer Theses and Dissertations Online Collection
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