Raman spectroscopic study on structure of human immunodeficiency virus (HIV) and hypericin-induced photosensitive damage of HIV.
The first Raman spectra of HIV1-HIV2 in human sera and hypericin-induced photosensitive damage of the virus have been obtained. The prominent Raman lines in the spectra are assigned respectively to the carbohydrates of viral glycoprotein, RNA, protein and lipid. The spectra are dominated by Raman scattering of the carbohydrates. The lines of D-Mannose and N-acetylglucosamine in carbohydrates are obvious and there is a beta-configuration in the anomeric C1 position in D-Mannose. The viral RNA duplexes bound assumes an A-form geometry. The lines of backbone phosphate group, bases (involving interbase hydrogen bonding) and ribose of the RNA are complete and distinct. The secondary structure of the viral protein maintains alpha-helix, beta-sheet, beta-turn and random coil. Its side chains are rich and vary from tryptophan, phenylalanine and "buried" tyrosine; the stable conformation of the S-S bond of gauche-gauche-gauche; the two forms of C-S bonds of gauche and trans; to sulfhydrl group and ionized and unionized carboxyl groups. The viral lipid bilayer molecules are probably in the liquid ordered phase or the gel phase. It was observed that the hypericin-induced photosensitive damage of HIV1-HIV2 in human sera changed various components of HIV1-HIV2 in different degrees: The orderly A-form viral RNA would become a disordered viral RNA. There were a breakage of interbase hydrogen bonds and disruption of vertical base-base stacking interactions. In addition, the groups of ribos and four bases were damaged obviously. A decrease in ordered structure (alpha-helix and beta-sheet) of viral protein is accompanied by an increase in random coil. The Tyr buried in the three-dimensional structure of protein was damaged, but it was still "buried" and the damage of C-S bond of trans form was stronger. The groups of carbohydrates, including D-Mannos and N-acetyl glucosamine, in viral envelope glycoprotein had also been changed. The hydrophilic C-N bond of choline in viral lipid was damaged, which was the possible binding site to hypericin, whereas the viral lipids bilayers were still probably in the liquid ordered phase or the gel phase. So the space structure of HIV1-HIV2 was damaged under the experimental conditions, which might block viral infection and inhibit its growth and breeding. It is apparent that the laser Raman spectra have provided certain direct evidence at the molecular level for photosensitive damage of HIV1-HIV2.
Laboratory of Visual Information Processing, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China. xuliang40@yahoo.com.cn
Yiming
Y
Xu
Chuanzong
C
Lu
D000873:Anthracenes; D006678:HIV / Q000737:chemistry*; D006679:HIV Seropositivity; D015497:HIV-1 / Q000737:chemistry; D015498:HIV-2 / Q000737:chemistry; D006801:Humans; D006860:Hydrogen Bonding; D008051:Lipid Bilayers / Q000032:analysis / Q000737:chemistry; D010569:Perylene / Q000031:analogs & derivatives* / Q000494:pharmacology; D010649:Phenylalanine / Q000737:chemistry; D017433:Protein Structure, Secondary; D012367:RNA, Viral / Q000032:analysis / Q000737:chemistry; D011838:Radiation-Sensitizing Agents / Q000494:pharmacology*; D013059:Spectrum Analysis, Raman; D014364:Tryptophan / Q000737:chemistry; D014443:Tyrosine / Q000737:chemistry; D014764:Viral Proteins / Q000032:analysis / Q000737:chemistry
D000873:Anthracenes; D008051:Lipid Bilayers; D012367:RNA, Viral; D011838:Radiation-Sensitizing Agents; D014764:Viral Proteins; D014443:Tyrosine; D010649:Phenylalanine; D010569:Perylene; C004965:hypericin; D014364:Tryptophan