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

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 81; no. 4; pp. 998 - 1002
• Main Authors: Lalor, T.M, Kjeldgaard, M, Shimamoto, G.T, Strickler, J.E, Konigsberg, W.H
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences of the United States of America 01.02.1984; National Acad Sciences
• Subjects: Amino Acid Sequence; Amino acids; Amino acids, Protozoa; Animals; Antibodies; antigenic variation; Biochemistry; cross reaction; Dichroism; Genes; Glycoproteins; Glycoproteins - genetics; Glycoproteins - isolation & purification; immunity; Infections; Isotypes; Molecular structure; Molecules; Parasite surfaces; Protein Conformation; Proteins, Protozoa; Protozoa; Trypanosoma brucei brucei - genetics; Trypanosoma brucei complex (Protozoa); Trypanosome; Variant Surface Glycoproteins, Trypanosoma
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.81.4.998

Trypanosoma brucei complex, analysis of secondary structure potential of five full-length and five partial amino acid sequences of variant-specific glycoproteins, potentials for alpha-helix, beta-turns, and beta-strand structure calculated, results imply that antigenic variation is mediated by 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 variant-specific glycoprotein family