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Antigenic and Structural Properties of Mutants in Herpes Simplex Virus 1 Glycoprotein B

  • Lenore Pereira
  • Ishtiaq Qadri
  • David Navarro
  • Concepcion Gimeno
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 278)

Abstract

The infectivity of herpes simplex viruses 1 and 2 (HSV-1 and HSV-2) is accomplished by the glycoproteins (g’s) in the virion envelope and is thought of as a two-step process. First, virions bind to host cells via a surface receptor molecule. Second, they enter cells by fusion of the virion envelope with the cell membrane. The structure of the viral glycoproteins has most likely evolved to optimize their role in infection. HSV-1 virions contain seven envelope glycoproteins (1–6). Four of these are not absolutely essential for growth in cell culture (6, 7); however, conditional lethal mutations in three—gB (8, 9), gH (4, 10), and gD (11)—preclude infectivity. Although gB and gD are the most abundant glycoproteins in HSV-1-infected cells, the topography of the glycoproteins assembled into the virion envelope has not been elucidated.

Keywords

Cysteine Residue Insertion Mutant None None Carboxy Terminus Continuous Domain 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1990

Authors and Affiliations

  • Lenore Pereira
    • 1
    • 2
  • Ishtiaq Qadri
    • 1
    • 2
  • David Navarro
    • 1
    • 2
  • Concepcion Gimeno
    • 1
    • 2
  1. 1.Department of Stomatology, School of DentistryUniversity of CaliforniaSan Francisco, San FranciscoUSA
  2. 2.Department of Microbiology and Immunology, School of MedicineUniversity of CaliforniaSan Francisco, San FranciscoUSA

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