Recognition molecules and immunoglobulin domains in invertebrates.
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.
Schluter
S F
SF
University of Arizona, College of Medicine, Tucson 85724.
Schroeder
J
J
Wang
E
E
Marchalonis
J J
JJ
D000595:Amino Acid Sequence; D000818:Animals; D005075:Biological Evolution; D017124:Conserved Sequence; D005260:Female; D006801:Humans; D007136:Immunoglobulins / Q000235:genetics*; D007448:Invertebrates / Q000235:genetics / Q000276:immunology*; D007798:Lampreys / Q000235:genetics / Q000276:immunology; D037102:Lectins / Q000235:genetics / Q000276:immunology; D008969:Molecular Sequence Data; D010063:Ovum / Q000276:immunology; D017386:Sequence Homology, Amino Acid; D014561:Urochordata / Q000235:genetics / Q000276:immunology
D007136:Immunoglobulins; D037102:Lectins