CiteULike is a free online bibliography manager. Register and you can start organising your references online.

A proline-rich structural protein of the surface sheath of larval Brugia filarial nematode parasites. Export

Journal of Biological Chemistry, Vol. 266 (1991), pp. 11002-11008.

Citation Format

[Posts]

View FullText article


C. elegans / WormBase's tags for this article

amino_acid_sequence article base_sequence blotting_northern blotting_western brugia_genetics brugia_growth_and_development brugia_physiology brugia_ultrastructure caenorhabditis_elegans celegans c_elegans cysteine electrophoresis_gel_two_dimensional electrophoresis_polyacrylamide_gel elegans helminth_proteins_genetics helminth_proteins_isolation_and_purification larva microscopy_immunoelectron molecular_sequence_data molecular_weight nematode protein_precursors_genetics protein_precursors_isolation_and_purification repetitive_sequences_nucleic_acid rna_genetics rna_isolation_and_purification sequence_homology_nucleic_acid signal_peptides_genetics wormbase

X Reviews [Write a review of this article]

X Find related articles from these CiteULike users

X Find related articles with these CiteULike tags

X Posting History

X Abstract

Both cDNA and genomic DNA sequences have been isolated which encode a proline-rich precursor protein of the sheath from microfilariae, the first stage larvae of the filarial nematode parasites Brugia pahangi and Brugia malayi. This 22-kDa protein is soluble only under reducing conditions and is extensively cross-linked by both disulfide and nonreducible bonds. Immunogold electron microscopy shows that the protein is localized exclusively in the sheath, a vestigial remnant of the eggshell, which is retained by and encloses the mature microfilaria. Analysis by Western blotting confirms that the protein is expressed only in microfilariae and adult female worms, although transcripts are detectable only in adult females. The deduced amino acid sequence contains a short N-terminal hydrophobic putative leader sequence, a central repetitive domain that contains 14 copies of a degenerate 5-amino acid repeat with the consensus sequence Met-Pro-Pro-Gln-Gly, and a C-terminal proline-rich domain flanked by clusters of cysteine residues. These clusters can be aligned with cysteine residues implicated in cross-linking of a family of cuticular collagens originally identified in Caenorhabditis elegans but which extends to other nematodes.


X BibTeX record

X RIS record


Privacy Statement | Terms & Conditions
CiteULike organises scholarly (or academic) papers or literature and provides bibliographic (which means it makes bibliographies) for universities and higher education establishments. It helps undergraduates and postgraduates. People studying for PhDs or in postdoctoral (postdoc) positions. The service is similar in scope to EndNote or RefWorks or any other reference manager like BibTeX, but it is a social bookmarking service for scientists and humanities researchers.