Acidic pH enhances structure and structural stability of the capsid protein of hepatitis E virus.
Hepatitis E virus (HEV) is enterically transmitted and endemic to tropical areas of the world. The major capsid protein of HEV is pORF2 ( approximately 74 kDa), encoded by open reading frame 2 (ORF2). When expressed in insect cells, it is processed into a approximately 55 kDa form (n-pORF2). We also generated a mutant, m-pORF2, lacking a C-terminal hydrophobic region shown earlier to be required for its homo-oligomerization. Circular dichroism was used to measure the secondary structure and stability of these proteins as a function of pH and temperature. With decreasing pH both proteins acquired increasing alpha-helicity and thermal stability in terms of midpoint of denaturation and the Gibbs energy change.
Zafrullah
Mohammad
M
Department of Biosciences, Jamia Millia Islamia, Jamia Nagar, New Delhi 110025, India.
Khursheed
Zenab
Z
Yadav
Sushma
S
Sahgal
Deepak
D
Jameel
Shahid
S
Ahmad
Faizan
F
D000818:Animals; D016367:Baculoviridae / Q000235:genetics; D036022:Capsid Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D002460:Cell Line; D002942:Circular Dichroism; D006023:Glycoproteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D016752:Hepatitis E virus / Q000737:chemistry*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D009036:Moths / Q000166:cytology; D011489:Protein Denaturation; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics; D013816:Thermodynamics
D036022:Capsid Proteins; D006023:Glycoproteins; D011994:Recombinant Proteins