title: Cytopathic mechanisms of HIV-1.
abstract: The human immunodeficiency virus type 1 (HIV-1) has been intensely investigated since its discovery in 1983 as the cause of acquired immune deficiency syndrome (AIDS). With relatively few proteins made by the virus, it is able to accomplish many tasks, with each protein serving multiple functions. The Envelope glycoprotein, composed of the two noncovalently linked subunits, SU (surface glycoprotein) and TM (transmembrane glycoprotein) is largely responsible for host cell recognition and entry respectively. While the roles of the N-terminal residues of TM is well established as a fusion pore and anchor for Env into cell membranes, the role of the C-terminus of the protein is not well understood and is fiercely debated. This review gathers information on TM in an attempt to shed some light on the functional regions of this protein.
authors.affiliation: Biotechnology Research Group, Department of Biology, Florida Gulf Coast University, 10501 FGCU Blvd, S., Fort Myers, Fl 33965, USA. jcostin@fgcu.edu
authors.forename: Joshua M
authors.initials: JM
authors.lastname: Costin
mesh_terms: D000818:Animals; D015496:CD4-Positive T-Lymphocytes / Q000276:immunology / Q000821:virology; D002460:Cell Line; D002463:Cell Membrane Permeability; D003588:Cytopathogenic Effect, Viral; D016679:Genome, Viral; D015700:HIV Envelope Protein gp41 / Q000737:chemistry* / Q000378:metabolism*; D015497:HIV-1 / Q000235:genetics / Q000378:metabolism / Q000472:pathogenicity* / Q000502:physiology; D006801:Humans; D007473:Ion Channels / Q000378:metabolism*; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism*; D012964:Sodium / Q000378:metabolism*; D014771:Virion / Q000378:metabolism; D014779:Virus Replication; D014981:Xenopus
chemical_list: D015700:HIV Envelope Protein gp41; D007473:Ion Channels; D010446:Peptide Fragments; C116049:lentiviral lytic peptide type 1, Human immunodeficiency virus 1; D012964:Sodium