Novel Monoclonal Antibodies for Studies of Human and Rhesus Macaque Secretory Component and Human J-Chain.

Journal Article (Journal Article)

Immunoglobulin A (IgA) antibodies exist in monomeric, dimeric, and secretory forms. Dimerization of IgA depends on a 15-kD polypeptide termed "joining (J) chain," which is also part of the binding site for an epithelial glycoprotein called "secretory component (SC)," whether this after apical cleavage on secretory epithelia is ligand bound in secretory IgA (SIgA) or in a free form. Uncleaved membrane SC, also called the "polymeric Ig receptor," is thus crucial for transcytotic export of SIgA to mucosal surfaces, where it interacts with and modulates commensal bacteria and mediates protective immune responses against exogenous pathogens. To evaluate different forms of IgA, we have produced mouse monoclonal antibodies (MAbs) against human J-chain and free SC. We found that J-chain MAb 9A8 and SC MAb 9H7 identified human dimeric IgA and SIgA in enzyme-linked immunoassay and western blot analysis, as well as functioning in immunohistochemistry to identify cytoplasmic IgA of intestinal lamina propria plasmablasts/plasma cells and crypt epithelium of distal human intestine. Finally, we demonstrated that SC MAb 9H7 cross-reacted with rhesus macaque SIgA. These novel reagents should be of use in the study of the biology of various forms of IgA in humans and SIgA in macaques, as well as in monitoring the production and/or isolation of these forms of IgA.

Full Text

Duke Authors

Cited Authors

  • Zhang, R; Alam, SM; Yu, J-S; Scearce, R; Lockwood, B; Hwang, K-K; Parks, R; Permar, S; Brandtzaeg, P; Haynes, BF; Liao, H-X

Published Date

  • August 2016

Published In

Volume / Issue

  • 35 / 4

Start / End Page

  • 217 - 226

PubMed ID

  • 27386924

Pubmed Central ID

  • PMC5003010

Electronic International Standard Serial Number (EISSN)

  • 2167-9436

Digital Object Identifier (DOI)

  • 10.1089/mab.2016.0014


  • eng

Conference Location

  • United States