scholarly journals Performance of the Focus and Kalon Enzyme-Linked Immunosorbent Assays for Antibodies to Herpes Simplex Virus Type 2 Glycoprotein G in Culture-Documented Cases of Genital Herpes

2003 ◽  
Vol 41 (11) ◽  
pp. 5212-5214 ◽  
Author(s):  
R. A. Morrow ◽  
D. Friedrich ◽  
E. Krantz
Viruses ◽  
2021 ◽  
Vol 13 (5) ◽  
pp. 887
Author(s):  
Edward Trybala ◽  
Nadia Peerboom ◽  
Beata Adamiak ◽  
Malgorzata Krzyzowska ◽  
Jan-Åke Liljeqvist ◽  
...  

The contribution of virus components to liberation of herpes simplex virus type 2 (HSV-2) progeny virions from the surface of infected cells is poorly understood. We report that the HSV-2 mutant deficient in the expression of a mucin-like membrane-associated glycoprotein G (mgG) exhibited defect in the release of progeny virions from infected cells manifested by ~2 orders of magnitude decreased amount of infectious virus in a culture medium as compared to native HSV-2. Electron microscopy revealed that the mgG deficient virions were produced in infected cells and present at the cell surface. These virions could be forcibly liberated to a nearly native HSV-2 level by the treatment of cells with glycosaminoglycan (GAG)-mimicking oligosaccharides. Comparative assessment of the interaction of mutant and native virions with surface-immobilized chondroitin sulfate GAG chains revealed that while the mutant virions associated with GAGs ~fourfold more extensively, the lateral mobility of bound virions was much poorer than that of native virions. These data indicate that the mgG of HSV-2 balances the virus interaction with GAG chains, a feature critical to prevent trapping of the progeny virions at the surface of infected cells.


2020 ◽  
Vol 198 ◽  
pp. 106200 ◽  
Author(s):  
Tomoaki Shima ◽  
Atsushi Nagaoka ◽  
Shunsuke Yoshimura ◽  
Akari Oka ◽  
Makiko Matsumoto ◽  
...  

2013 ◽  
Vol 85 (10) ◽  
pp. 1818-1828 ◽  
Author(s):  
Tohru Daikoku ◽  
Kazuhiro Horiba ◽  
Takashi Kawana ◽  
Masaru Hirano ◽  
Kimiyasu Shiraki

Sign in / Sign up

Export Citation Format

Share Document