Understanding HSV-1 entry glycoproteins.
Herpes Simplex Virus-1 is a common infectious agent, but the precise detail of entry and infection of cells has only now begun to be clarified. Four viral surface glycoproteins (gB, gD, gH and gL) are required. This review summarises the known structure and function of each of these essential viral envelope glycoproteins, and explores what is known about their close cooperation with each other in mediating cellular membrane fusion. It is suggested that, following gD binding to one of its entry receptors, membrane fusion is mediated by gB and the heterodimer gH/gL. Significantly, these four entry glycoproteins also play a key role in the interaction between HSV and the host immune system. The glycoproteins serve an important role as targets of adaptive immunity. However, recent studies have demonstrated that the same proteins also play a key role in initiating the early innate immune response to HSV. Understanding the complex functions of these HSV proteins may be essential for successful development of vaccines for HSV.
Reske
Adi
A
Department of Immunology and Molecular Pathology, Windeyer Institute of Medical Sciences, University College London, London, UK.
Pollara
Gabriele
G
Krummenacher
Claude
C
Chain
Benjamin M
BM
Katz
David R
DR
D018259:Herpesvirus 1, Human / Q000502:physiology*; D006801:Humans; D014759:Viral Envelope Proteins / Q000737:chemistry* / Q000502:physiology*; D053586:Virus Internalization
D014759:Viral Envelope Proteins; C040495:glycoprotein B, Simplexvirus; C044200:glycoprotein H, herpes simplex virus type 1; C077407:glycoprotein L, Human herpesvirus 1; C515577:glycoprotein gD, herpes simplex virus type 1