TY - JOUR T1 - The Major Envelope Glycoprotein of Murid Herpesvirus 4 Promotes Sexual Transmission. JF - J Virol Y1 - 2017 A1 - Zeippen, Caroline A1 - Javaux, Justine A1 - Xiao, Xue A1 - Ledecq, Marina A1 - Mast, Jan A1 - Farnir, Frédéric A1 - Vanderplasschen, Alain A1 - Stevenson, Philip A1 - Gillet, Laurent KW - Animals KW - Disease Transmission, Infectious KW - Glycoproteins KW - Herpesviridae Infections KW - Rhadinovirus KW - Sexually Transmitted Diseases, Viral KW - Viral Envelope Proteins KW - Virus Attachment KW - Virus Internalization KW - Virus Release AB -

Gammaherpesviruses are important human and animal pathogens. Infection control has proven difficult because the key process of transmission is ill understood. Murid herpesvirus 4 (MuHV-4), a gammaherpesvirus of mice, is transmitted sexually. We show that this depends on the major virion envelope glycoprotein gp150. gp150 is redundant for host entry, and , it regulates rather than promotes cell binding. We show that gp150-deficient MuHV-4 reaches and replicates normally in the female genital tract after nasal infection but is poorly released from vaginal epithelial cells and fails to pass from the female to the male genital tract during sexual contact. Thus, we show that the regulation of virion binding is a key component of spontaneous gammaherpesvirus transmission. Gammaherpesviruses are responsible for many important diseases in both animals and humans. Some important aspects of their life cycle are still poorly understood. Key among these is viral transmission. Here we show that the major envelope glycoprotein of murid herpesvirus 4 functions not in entry or dissemination but in virion release to allow sexual transmission to new hosts.

VL - 91 CP - 13 U1 - https://www.ncbi.nlm.nih.gov/pubmed/28424280?dopt=Abstract M3 - 10.1128/JVI.00235-17 ER -