Four-sector tandem mass spectrometric analysis of complex mixtures of phosphatidylcholines present in a human immunodeficiency virus preparation

• Published in: Analytical chemistry (Washington) Vol. 63; no. 11; pp. 1110 - 1114
• Main Authors: Bryant, Duncan K, Orlando, Ronald C, Fenselau, Catherine, Sowder, Raymond C, Henderson, Louis E
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 01.06.1991
• Subjects: AIDS/HIV; Biological and medical sciences; Fundamental and applied biological sciences. Psychology; HIV-1 - analysis; Humans; Mass Spectrometry; Microbiology; Miscellaneous; Phosphatidylcholines - analysis; Virology; Virus; Biological preparation; HIV-1 virus; Mass spectrometry MS/MS; Retroviridae; HPLC chromatography; Phosphatidylcholine; FAB mass spectrum; Lentivirinae; Qualitative analysis; Human immunodeficiency virus
• ISSN: 0003-2700; 1520-6882
• DOI: 10.1021/ac00011a010

A number of phosphatidylcholines have been isolated from an HIV-1/MN preparation by reversed-phase high-performance liquid chromatography (HPLC) and analyzed by fast atom bombardment mass spectrometry (FABMS), FABMS/MS, and FABMS/MS/MS in both positive- and negative-ion modes. Negative-ion FABMS/MS with high-energy collisions was used to identify the length of the acyl groups and the degree of saturation, as well as their position on the glyceride group. FABMS/MS in the positive-ion mode was used to identify the polar head group. Negative-ion FABMS/MS/MS was used to locate positions of double bonds in acyl groups. We find that four-sector tandem mass spectrometry with high-energy collisional activation provides qualitative analysis of viral phosphatidyl lipids in considerable detail, as well as semiquantitative information. Approximate quantitation of the phosphatidylcholine content of the HIV-1/MN preparation by measuring relative peak heights of molecular ions in FABMS reveals an array of phosphatidylcholines consistent with that found in human erythrocytes, indicating the likely source of lipids in the viral membrane to be the host cell membrane.