Recognition molecules and immunoglobulin domains in invertebrates

S. F. Schluter, Joyce Schroeder, E. Wang, J. J. Marchalonis

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

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 (μCRM) reacts with antibodies raised to shark IgM heavy chains. Intact tunicate μCRM 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.

Original languageEnglish (US)
Pages (from-to)74-81
Number of pages8
JournalAnnals of the New York Academy of Sciences
Volume712
StatePublished - 1994

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Urochordata
Invertebrates
Immunoglobulins
Molecules
C-Type Lectins
Lampreys
Sequence Homology
Mammals
Antibodies
Sharks
Peptides
Hemolymph
Cell Extracts
T-cells
Lectins
Immunoglobulin M
Polymers
Western Blotting
Immunoglobulin Domains
T-Lymphocytes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Recognition molecules and immunoglobulin domains in invertebrates. / Schluter, S. F.; Schroeder, Joyce; Wang, E.; Marchalonis, J. J.

In: Annals of the New York Academy of Sciences, Vol. 712, 1994, p. 74-81.

Research output: Contribution to journalArticle

Schluter, S. F. ; Schroeder, Joyce ; Wang, E. ; Marchalonis, J. J. / Recognition molecules and immunoglobulin domains in invertebrates. In: Annals of the New York Academy of Sciences. 1994 ; Vol. 712. pp. 74-81.
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