LL-37observational2001

Rhesus monkey (Macaca mulatta) mucosal antimicrobial peptides are close homologues of human molecules.

Clinical and diagnostic laboratory immunology

confidence

Key findings

Cloned and characterized rhesus monkey homologues (rhBD-1, rhBD-2, rhLL-37/rhCAP-18) showing high homology to human antimicrobial peptides; molecular characterization study.

View source on PubMed (PMID 11238224) ↗

Sample size
not_reported
Population
Rhesus monkey (Macaca mulatta) tissues
Dosing
not_applicable
Duration
not_reported
Route
not_applicable
Blinding
not_reported
Controls
none
Drug class
antimicrobial peptide
Full abstract

One component of host defense at mucosal surfaces appears to be epithelium-derived antimicrobial peptides. Molecules of the defensin and cathelicidin families have been studied in several species, including human and mouse. We describe in this report the identification and characterization of rhesus monkey homologues of human mucosal antimicrobial peptides. Using reverse transcriptase PCR methodology, we cloned the cDNAs of rhesus monkey beta-defensin 1 and 2 (rhBD-1 and rhBD-2) and rhesus monkey LL-37/CAP-18 (rhLL-37/rhCAP-18). The predicted amino acid sequences showed a high degree of homology to the human molecules. The expression of the monkey antimicrobial peptides was analyzed using immunohistochemistry with three polyclonal antibodies to the human molecules. As in humans, rhesus monkey antimicrobial peptides are expressed in epithelia of various organs. The present study demonstrates that beta-defensins and cathelicidins of rhesus monkeys are close homologues to the human molecules and indicate that nonhuman primates represent valid model organisms to study innate immune functions.

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