Trypanosoma congolense: structure and molecular organization of the surface glycoproteins of two early bloodstream variants. 1987

J E Strickler, and D A Binder, and J J L'Italien, and G T Shimamoto, and S W Wait, and L J Dalheim, and J Novotny, and J A Radding, and W H Konigsberg, and M Y Armstrong

The complete primary structures of two variant specific glycoproteins (VSGs) of the nannomonad Trypanosoma (N.) congolense are presented. These coat proteins subserve the function of antigenic variation. The secondary structure potentials of both VSGs have been calculated. The amino acid sequences and secondary structure potentials of these VSGs have been compared with the primary structures and secondary structure potentials of several Trypanosoma brucei complex VSGs. In homologous regions, the T. brucei complex VSGs show a pattern of sharply contrasting secondary structure potentials. It has been suggested previously that this pattern gives rise to different folding structures in different members of this polygene protein family. Thus, different short regions of the polypeptide sequence are exposed as antigenic "caps" on the solvent-exposed surface of intact trypanosomes. A sharply contrasting secondary structure potential pattern is also found in regions of the two T. congolense VSGs. However, there is little homology of primary structure between each of the two T. congolense VSGs and any member of the T. brucei complex VSG polygene family whose primary structure has been determined.

UI MeSH Term Description Entries
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D003001 Cloning, Molecular The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells. Molecular Cloning
D004247 DNA A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine). DNA, Double-Stranded,Deoxyribonucleic Acid,ds-DNA,DNA, Double Stranded,Double-Stranded DNA,ds DNA
D006023 Glycoproteins Conjugated protein-carbohydrate compounds including MUCINS; mucoid, and AMYLOID glycoproteins. C-Glycosylated Proteins,Glycosylated Protein,Glycosylated Proteins,N-Glycosylated Proteins,O-Glycosylated Proteins,Glycoprotein,Neoglycoproteins,Protein, Glycosylated,Proteins, C-Glycosylated,Proteins, Glycosylated,Proteins, N-Glycosylated,Proteins, O-Glycosylated
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001483 Base Sequence The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence. DNA Sequence,Nucleotide Sequence,RNA Sequence,DNA Sequences,Base Sequences,Nucleotide Sequences,RNA Sequences,Sequence, Base,Sequence, DNA,Sequence, Nucleotide,Sequence, RNA,Sequences, Base,Sequences, DNA,Sequences, Nucleotide,Sequences, RNA
D012689 Sequence Homology, Nucleic Acid The sequential correspondence of nucleotides in one nucleic acid molecule with those of another nucleic acid molecule. Sequence homology is an indication of the genetic relatedness of different organisms and gene function. Base Sequence Homology,Homologous Sequences, Nucleic Acid,Homologs, Nucleic Acid Sequence,Homology, Base Sequence,Homology, Nucleic Acid Sequence,Nucleic Acid Sequence Homologs,Nucleic Acid Sequence Homology,Sequence Homology, Base,Base Sequence Homologies,Homologies, Base Sequence,Sequence Homologies, Base
D014348 Trypanosoma congolense A species of Trypanosome hemoflagellates that is carried by tsetse flies and causes severe anemia in cattle. These parasites are also found in horses, sheep, goats, and camels. Trypanosoma (Nannomonas) congolense,Trypanosoma congolenses,congolense, Trypanosoma
D014643 Variant Surface Glycoproteins, Trypanosoma Glycoproteins attached to the surface coat of the trypanosome. Many of these glycoproteins show amino acid sequence diversity expressed as antigenic variations. This continuous development of antigenically distinct variants in the course of infection ensures that some trypanosomes always survive the development of immune response to propagate the infection. Surface Variant Glycoproteins, Trypanosoma,Trypanosoma Variant Surface Coat Glycoproteins,SSP-4,VSG 117,VSG 118,VSG 221

Related Publications

J E Strickler, and D A Binder, and J J L'Italien, and G T Shimamoto, and S W Wait, and L J Dalheim, and J Novotny, and J A Radding, and W H Konigsberg, and M Y Armstrong
February 1982, Experimental parasitology,
J E Strickler, and D A Binder, and J J L'Italien, and G T Shimamoto, and S W Wait, and L J Dalheim, and J Novotny, and J A Radding, and W H Konigsberg, and M Y Armstrong
December 1981, Experimental parasitology,
J E Strickler, and D A Binder, and J J L'Italien, and G T Shimamoto, and S W Wait, and L J Dalheim, and J Novotny, and J A Radding, and W H Konigsberg, and M Y Armstrong
October 1981, Experimental parasitology,
J E Strickler, and D A Binder, and J J L'Italien, and G T Shimamoto, and S W Wait, and L J Dalheim, and J Novotny, and J A Radding, and W H Konigsberg, and M Y Armstrong
April 1981, Federation proceedings,
J E Strickler, and D A Binder, and J J L'Italien, and G T Shimamoto, and S W Wait, and L J Dalheim, and J Novotny, and J A Radding, and W H Konigsberg, and M Y Armstrong
January 1987, Molecular and biochemical parasitology,
J E Strickler, and D A Binder, and J J L'Italien, and G T Shimamoto, and S W Wait, and L J Dalheim, and J Novotny, and J A Radding, and W H Konigsberg, and M Y Armstrong
May 1992, The Journal of biological chemistry,
J E Strickler, and D A Binder, and J J L'Italien, and G T Shimamoto, and S W Wait, and L J Dalheim, and J Novotny, and J A Radding, and W H Konigsberg, and M Y Armstrong
February 1969, The Journal of protozoology,
J E Strickler, and D A Binder, and J J L'Italien, and G T Shimamoto, and S W Wait, and L J Dalheim, and J Novotny, and J A Radding, and W H Konigsberg, and M Y Armstrong
March 2017, Microbial cell (Graz, Austria),
J E Strickler, and D A Binder, and J J L'Italien, and G T Shimamoto, and S W Wait, and L J Dalheim, and J Novotny, and J A Radding, and W H Konigsberg, and M Y Armstrong
November 1993, Infection and immunity,
J E Strickler, and D A Binder, and J J L'Italien, and G T Shimamoto, and S W Wait, and L J Dalheim, and J Novotny, and J A Radding, and W H Konigsberg, and M Y Armstrong
June 1985, Molecular and biochemical parasitology,
Copied contents to your clipboard!