Recognition molecules and immunoglobulin domains in invertebrates.

Published

Journal Article

We have used specific antibody probes to conserved antigenic motifs to identify and characterize immunoglobulin-related molecules in tunicates and a C-type lectin found in lamprey that is related to molecules found in tunicates and mammals. The tunicate immunoglobulin cross-reactive molecule (mu CRM) reacts with antibodies raised to shark IgM heavy chains. Intact tunicate mu CRM is a monomer of Ig light-chain-sized subunits and is oligoclonal by IEF. That this molecule is related to Ig is indicated both by immunochemical data and by peptide sequence homologies. The lamprey lectin is a large polymer (> 500,000 kDa) of 35-kDa and 60-kDa subunits. It appears to be related to C-type lectins as shown by peptide sequence homology and the requirement of Ca2+ for activity. Related molecules appear to be present in tunicates and mammals as shown by cross-reactivity of antibodies in Western blots with single bands from hemolymph and T-cell extracts.

Full Text

Duke Authors

Cited Authors

  • Schluter, SF; Schroeder, J; Wang, E; Marchalonis, JJ

Published Date

  • April 15, 1994

Published In

Volume / Issue

  • 712 /

Start / End Page

  • 74 - 81

PubMed ID

  • 8192354

Pubmed Central ID

  • 8192354

International Standard Serial Number (ISSN)

  • 0077-8923

Digital Object Identifier (DOI)

  • 10.1111/j.1749-6632.1994.tb33563.x

Language

  • eng

Conference Location

  • United States