Thermostability of the HIV gp41 wild-type and loop mutations.
The HIV and SIV gp41 ectodomains are extremely stable to chemical and thermal denaturation and the observed stability has been proposed to be an important thermodynamic driving force for gp41-mediated fusion of the viral and target cell membranes. The importance of the disulphide bond and surrounding residues within the HIV gp41 loop have been assayed by DSC studies of wild type and mutant HIV gp41. Based on the thermal transition temperature, the disulphide bond and surrounding residues do not contribute to the thermal stability of gp41 and thus do not contribute to gp41-mediated membrane fusion.
Jacobs
Amy
A
Department of Biochemistry and Molecular Genetics,University of Illinois at Chicago, Chicago, IL 60607, USA.
Simon
Cecile
C
Caffrey
Michael
M
D000818:Animals; D002151:Calorimetry; D004220:Disulfides / Q000737:chemistry; D004795:Enzyme Stability; D015700:HIV Envelope Protein gp41 / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D006801:Humans; D008561:Membrane Fusion; D008562:Membrane Glycoproteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D009154:Mutation; D011489:Protein Denaturation; D017434:Protein Structure, Tertiary; D012191:Retroviridae Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013696:Temperature; D013816:Thermodynamics
D004220:Disulfides; D015700:HIV Envelope Protein gp41; D008562:Membrane Glycoproteins; D012191:Retroviridae Proteins; C082614:SIV envelope protein gp41