Reference : Hiv-1 Gp41 And Gp160 Are Hyperthermostable Proteins In A Mesophilic Environment - Cha...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Hiv-1 Gp41 And Gp160 Are Hyperthermostable Proteins In A Mesophilic Environment - Characterization Of Gp41 Mutants
Krell, Tino [Aventis Pasteur (Marcy l’Etoile, France) > > >]
Greco, Frédéric [Aventis Pasteur (Marcy l’Etoile, France) > > >]
Engel, Olivier [Aventis Pasteur (Marcy l’Etoile, France) > > >]
Dubayle, Jean [Aventis Pasteur (Marcy l’Etoile, France) > > >]
Dubayle, Joseline [Aventis Pasteur (Marcy l’Etoile, France) > > >]
Kennel, Audrey [Aventis Pasteur (Marcy l’Etoile, France) > > >]
Charloteaux, Benoît [Université de Liège - ULg > > Gembloux Agro-Bio Tech >]
Brasseur, Robert mailto [Université de Liège - ULg > > Gembloux Agro-Bio Tech >]
Chevalier, Michel [Aventis Pasteur (Marcy l’Etoile, France) > > >]
Sodoyer, Régis [Aventis Pasteur (Marcy l’Etoile, France) > > >]
El Habib, Raphaëlle [Aventis Pasteur (Marcy l’Etoile, France) > > >]
European Journal of Biochemistry
Yes (verified by ORBi)
[en] HIV gp41(24-157) unfolds cooperatively over the pH range of 1.0-4.0 with T(m)
values of > 100 degrees C. At pH 2.8, protein unfolding was 80% reversible and
the DeltaH(vH)/DeltaH(cal) ratio of 3.7 is indicative of gp41 being trimeric. No
evidence for a monomer-trimer equilibrium in the concentration range of 0.3-36
micro m was obtained by DSC and tryptophan fluorescence. Glycosylation of gp41
was found to have only a marginal impact on the thermal stability. Reduction of
the disulfide bond or mutation of both cysteine residues had only a marginal
impact on protein stability. There was no cooperative unfolding event in the DSC
thermogram of gp160 in NaCl/P(i), pH 7.4, over a temperature range of 8-129
degrees C. When the pH was lowered to 5.5-3.4, a single unfolding event at around
120 degrees C was noted, and three unfolding events at 93.3, 106.4 and 111.8
degrees C were observed at pH 2.8. Differences between gp41 and gp160, and
hyperthermostable proteins from thermophile organisms are discussed. A series of
gp41 mutants containing single, double, triple or quadruple point mutations were
analysed by DSC and CD. The impact of mutations on the protein structure, in the
context of generating a gp41 based vaccine antigen that resembles a fusion
intermediate state, is discussed. A gp41 mutant, in which three hydrophobic amino
acids in the gp41 loop were replaced with charged residues, showed an increased
solubility at neutral pH.
Researchers ; Professionals

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