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Structural and Functional Comparisons of Retroviral Envelope Protein C-Terminal Domains: Still Much to Learn
Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261, USA
Center for Vaccine Research, University of Pittsburgh, Pittsburgh, PA 15261, USA
* Author to whom correspondence should be addressed.
Received: 31 October 2013; Accepted: 6 January 2014 / Published: 16 January 2014
Abstract: Retroviruses are a family of viruses that cause a broad range of pathologies in animals and humans, from the apparently harmless, long-term genomic insertion of endogenous retroviruses, to tumors induced by the oncogenic retroviruses and acquired immunodeficiency syndrome (AIDS) resulting from human immunodeficiency virus infection. Disease can be the result of diverse mechanisms, including tumorigenesis induced by viral oncogenes or immune destruction, leading to the gradual loss of CD4 T-cells. Of the virally encoded proteins common to all retroviruses, the envelope (Env) displays perhaps the most diverse functionality. Env is primarily responsible for binding the cellular receptor and for effecting the fusion process, with these functions mediated by protein domains localized to the exterior of the virus. The remaining C-terminal domain may have the most variable functionality of all retroviral proteins. The C-terminal domains from three prototypical retroviruses are discussed, focusing on the different structures and functions, which include fusion activation, tumorigenesis and viral assembly and lifecycle influences. Despite these genetic and functional differences, however, the C-terminal domains of these viruses share a common feature in the modulation of Env ectodomain conformation. Despite their differences, perhaps each system still has information to share with the others.
Keywords: retroviruses; HIV; MuLV; JSRV; cytoplasmic domain; C-terminal tail
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MDPI and ACS Style
Steckbeck, J.D.; Kuhlmann, A.-S.; Montelaro, R.C. Structural and Functional Comparisons of Retroviral Envelope Protein C-Terminal Domains: Still Much to Learn. Viruses 2014, 6, 284-300.
Steckbeck JD, Kuhlmann A-S, Montelaro RC. Structural and Functional Comparisons of Retroviral Envelope Protein C-Terminal Domains: Still Much to Learn. Viruses. 2014; 6(1):284-300.
Steckbeck, Jonathan D.; Kuhlmann, Anne-Sophie; Montelaro, Ronald C. 2014. "Structural and Functional Comparisons of Retroviral Envelope Protein C-Terminal Domains: Still Much to Learn." Viruses 6, no. 1: 284-300.