Interaction of fibronectin with semen amyloids synergistically enhances HIV infection.
Semen harbors amyloids that enhance human immunodeficiency virus type 1 (HIV-1) infection. We set out to identify factors that bind these amyloids and to determine whether these factors modulate amyloid-mediated HIV-enhancing activity. Using biochemical and mass spectrometric approaches, we identified fibronectin as a consistent interaction partner. Although monomeric fibronectin did not enhance HIV infection, it synergistically increased the infectivity enhancement activity of the amyloids. Depletion of fibronectin decreased the enhancing activity of semen, suggesting that interfering with the binding interface between fibronectin and the amyloids could be an approach to developing a novel class of microbicides targeting the viral-enhancing activity of semen.
Gladstone Institute of Virology and Immunology Department of Urology.
Nadia R
NR
Roan
Gladstone Institute of Virology and Immunology.
Simon
S
Chu
Department of Obstetrics, Gynecology, and Reproductive Sciences Sandler-Moore Mass Spectrometry Core Facility.
Haichuan
H
Liu
Gladstone Institute of Virology and Immunology.
Jason
J
Neidleman
Department of Obstetrics, Gynecology, and Reproductive Sciences Sandler-Moore Mass Spectrometry Core Facility.
H Ewa
HE
Witkowska
Gladstone Institute of Virology and Immunology Department of Medicine Department of Microbiology and Immunology, University of California, San Francisco.
Warner C
WC
Greene
D000682:Amyloid / Q000378:metabolism*; D005353:Fibronectins / Q000378:metabolism*; D015497:HIV-1 / Q000502:physiology*; D006801:Humans; D011485:Protein Binding; D012661:Semen / Q000737:chemistry* / Q000821:virology*; D053586:Virus Internalization
D000682:Amyloid; D005353:Fibronectins
HIV; SEVI; amyloid; fibronectin; semen; semenogelin