NDLI: Trypanosome variant-specific glycoproteins: a polygene protein family with multiple folding patterns?

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Trypanosome variant-specific glycoproteins: a polygene protein family with multiple folding patterns?

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Trypanosome variant-specific glycoproteins: a polygene protein family with multiple folding patterns?

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Kjeldgaard, M. Strickler, J. E. Richards, F. F. Lalor, T. M. Konigsberg, W. H. Shimamoto, G. T.
Abstract	Infection with the African trypanosomes gives rise to relapsing waves of parasitemia in the host. A predominant population of trypanosomes is present in each wave, and such predominant populations are usually serologically distinct from each other. Trypanosomes are covered by an extramembranous, highly antigenic, variant-specific glycoprotein coat that is 15 nm thick. The primary structure of a large portion of the glycoprotein molecule is different in the predominant trypanosome populations of each parasitemic wave. Analysis of the secondary structure potential of five full-length and five partial amino acid sequences of variant-specific glycoproteins from members of the Trypanosoma brucei complex has been carried out. The potentials for alpha-helix, beta-turns, and beta-strand structure have been calculated. A high degree of alpha-helical structure potential is present in all the full-length or partial sequences examined. There is conservation of secondary structure potential in the COOH-terminal 100 amino acids, where both partial and complete conservation of primary amino acid sequence exists. The NH2-terminal regions are rich in alpha-helix potential. However, over large stretches of the middle of the VSG molecules there is wide diversity of secondary structure potential. This suggests that tertiary folding structures may also be different in this region. If these predictions are true, different regions of the variant-specific glycoprotein could be exposed to the solvent in different variant-specific trypanosome serotypes. The implication is that antigenic variation is mediated by a polygene family of glycoproteins containing highly polymorphic regions. These could fold differently and expose different surface regions of the protein to the solvent. This device might reduce immune crossreactivity among members of the variant-specific glycoprotein family.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	4
Volume Number	81
Language	English
Publisher	National Academy of Sciences
Publisher Date	1984-04-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Genes Glycoproteins Genetics Protein Conformation Trypanosoma Brucei Brucei Amino Acid Sequence Animals Isolation & Purification Variant Surface Glycoproteins, Trypanosoma Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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