Abstract
The interferon-induced BST-2 protein has the unique ability to restrict the egress of HIV-1, Kaposi's sarcoma–associated herpesvirus (KSHV), Ebola virus, and other enveloped viruses. The observation that virions remain attached to the surface of BST-2-expressing cells led to the renaming of BST-2 as “tetherin”. However, viral proteins such as HIV-1 Vpu, simian immunodeficiency virus Nef, and KSHV K5 counteract BST-2, thereby allowing mature virions to readily escape from infected cells. Since the anti-viral function of BST-2 was discovered, there has been an explosion of research into several aspects of this intriguing interplay between host and virus. This review focuses on recent work addressing the molecular mechanisms involved in BST-2 restriction of viral egress and the species-specific countermeasures employed by various viruses.
Highlights
BST-2 (CD317/HM1.24) was initially identified by two independent groups searching for novel surface markers of terminally differentiated normal and neoplastic B cells [1,2]
We focus primarily on human BST-2 and HIV-1 to describe the molecular characteristics of BST-2, countermeasures employed by HIV-1 Vpu, and the genetic and mechanistic aspects of the host–virus interaction
N beta transducin repeat-containing protein (bTrCP)-dependent, proteasomal BST-2 degradation N bTrCP-dependent lysosomal BST-2 degradation N Vpu acts upon BST-2 at the plasma membrane N Vpu binds to BST-2 via their TM domains
Summary
BST-2 (CD317/HM1.24) was initially identified by two independent groups searching for novel surface markers of terminally differentiated normal and neoplastic B cells [1,2]. The function of BST2 remained unknown until it was identified as an intrinsic antiviral factor that restricts the egress of HIV-1 by tethering mature virions to the host cell surface [4]. A recent report has identified BCA2 as a BST-2interacting factor, which is thought to supplement the BST-2 viral restriction by enhancing the internalization and degradation of tethered virions from the cell surface [18].
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