Hiv env proteins: Difference between revisions

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== Introduction ==

Human Immunodeficiency Virus (HIV) is a retrovirus/lentivirus that expresses a spike protein on its viral envelope (Env). "The envelope protein is synthesized as a precursor, gp160, which trimerizes and undergoes cleavage into two noncovalently associated fragments, the receptor-binding fragment gp120 and the fusion fragment gp41" <ref name=Guan>PMID: 21076402 </ref>. Thus, Env is a heterodimer consisting of gp120 and gp41 and forms trimers on the surface of the viral membrane. As "the sole antigen on the virion surface," an understanding of Env (gp 120 & 41) and the conformational changes that occur in gp120 and gp41 during binding and fusion, respectively, is necessary in developing new fusion inhibitors and possible vaccines <ref name=Guan>PMID: 21076402 </ref> <ref name=Nick>PMID: 18668044 </ref>. The protein structure shown on the right is the gp120 portion of Env in its unbound trimer state <ref name=Nick>PMID: 18668044 </ref>.

Human Immunodeficiency Virus (HIV) is a retrovirus/lentivirus that expresses a spike protein on its viral envelope '''(Env)'''. "The envelope protein is synthesized as a precursor, gp160, which trimerizes and undergoes cleavage into two noncovalently associated fragments, the receptor-binding fragment gp120 and the fusion fragment gp41" <ref name=Guan>PMID: 21076402 </ref>. Thus, Env is a heterodimer consisting of gp120 and gp41 and forms trimers on the surface of the viral membrane. As "the sole antigen on the virion surface," an understanding of Env (gp 120 & 41) and the conformational changes that occur in gp120 and gp41 during binding and fusion, respectively, is necessary in developing new fusion inhibitors and possible vaccines <ref name=Guan>PMID: 21076402 </ref> <ref name=Nick>PMID: 18668044 </ref>. The protein structure shown on the right is the gp120 portion of Env in its unbound trimer state <ref name=Nick>PMID: 18668044 </ref>.

Hiv env proteins: Difference between revisions

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 <StructureSection load='3dnn' size='400' side='right' caption='Molecular structure for the HIV-1 gp120 trimer in the unliganded state (PDB entry [[3dnn]])' scene=''>
 == Introduction ==
-Human Immunodeficiency Virus (HIV) is a retrovirus/lentivirus that expresses a spike protein on its viral envelope (Env). "The envelope protein is synthesized as a precursor, gp160, which trimerizes and undergoes cleavage into two noncovalently associated fragments, the receptor-binding fragment gp120 and the fusion fragment gp41" <ref name=Guan>PMID: 21076402 </ref>. Thus, Env is a heterodimer consisting of gp120 and gp41 and forms trimers on the surface of the viral membrane. As "the sole antigen on the virion surface," an understanding of Env (gp 120 & 41) and the conformational changes that occur in gp120 and gp41 during binding and fusion, respectively, is necessary in developing new fusion inhibitors and possible vaccines <ref name=Guan>PMID: 21076402 </ref> <ref name=Nick>PMID: 18668044 </ref>. The protein structure shown on the right is the gp120 portion of Env in its unbound trimer state <ref name=Nick>PMID: 18668044 </ref>.
+Human Immunodeficiency Virus (HIV) is a retrovirus/lentivirus that expresses a spike protein on its viral envelope '''(Env)'''. "The envelope protein is synthesized as a precursor, gp160, which trimerizes and undergoes cleavage into two noncovalently associated fragments, the receptor-binding fragment gp120 and the fusion fragment gp41" <ref name=Guan>PMID: 21076402 </ref>. Thus, Env is a heterodimer consisting of gp120 and gp41 and forms trimers on the surface of the viral membrane. As "the sole antigen on the virion surface," an understanding of Env (gp 120 & 41) and the conformational changes that occur in gp120 and gp41 during binding and fusion, respectively, is necessary in developing new fusion inhibitors and possible vaccines <ref name=Guan>PMID: 21076402 </ref> <ref name=Nick>PMID: 18668044 </ref>. The protein structure shown on the right is the gp120 portion of Env in its unbound trimer state <ref name=Nick>PMID: 18668044 </ref>.