Chicken cathelicidin-B1, an antimicrobial guardian at the mucosal M cell gateway

Mucosal epithelial M cells provide an efficient portal of entry for microorganisms. Initially defined by their irregular microvilli and abundant transcytotic channels in the avian bursa of Fabricius, M cells also are found in the lymphoid follicle-associated epithelium of the mammalian appendix, Pey...

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Published inProceedings of the National Academy of Sciences - PNAS Vol. 104; no. 38; pp. 15063 - 15068
Main Authors Goitsuka, Ryo, Chen, Chen-lo H, Benyon, Lesley, Asano, Yusuke, Kitamura, Daisuke, Cooper, Max D
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences 18.09.2007
National Acad Sciences
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Abstract Mucosal epithelial M cells provide an efficient portal of entry for microorganisms. Initially defined by their irregular microvilli and abundant transcytotic channels in the avian bursa of Fabricius, M cells also are found in the lymphoid follicle-associated epithelium of the mammalian appendix, Peyer's patches, and other mucosal surface-lymphoid interfaces. We describe here a previously unrecognized cathelicidin gene in chickens, chCATH-B1, that is expressed exclusively in the epithelium of the bursa of Fabricius. Like the mature peptides of previously identified cathelicidins, the carboxyl-terminal peptide of chCATH-B1 has broad antimicrobial activity against Gram-positive and Gram-negative bacteria. chCATH-B1 expression is restricted to the secretory epithelial cell neighbors of the M cells, whereas its mature peptide is transported to become concentrated on the fibrillar network surrounding basolateral surfaces of the M cells that overlie the bursal lymphoid follicles. We conclude that chCATH-B1 is well placed to serve a protective antimicrobial role at the M cell gateway.
AbstractList Mucosal epithelial M cells provide an efficient portal of entry for microorganisms. Initially defined by their irregular microvilli and abundant transcytotic channels in the avian bursa of Fabricius, M cells also are found in the lymphoid follicle-associated epithelium of the mammalian appendix, Peyer's patches, and other mucosal surface-lymphoid interfaces. We describe here a previously unrecognized cathelicidin gene in chickens, chCATH-B1, that is expressed exclusively in the epithelium of the bursa of Fabricius. Like the mature peptides of previously identified cathelicidins, the carboxyl-terminal peptide of chCATH-B1 has broad antimicrobial activity against Gram-positive and Gram-negative bacteria. chCATH-B1 expression is restricted to the secretory epithelial cell neighbors of the M cells, whereas its mature peptide is transported to become concentrated on the fibrillar network surrounding basolateral surfaces of the M cells that overlie the bursal lymphoid follicles. We conclude that chCATH-B1 is well placed to serve a protective antimicrobial role at the M cell gateway. [PUBLICATION ABSTRACT]
Mucosal epithelial M cells provide an efficient portal of entry for microorganisms. Initially defined by their irregular microvilli and abundant transcytotic channels in the avian bursa of Fabricius, M cells also are found in the lymphoid follicle-associated epithelium of the mammalian appendix, Peyer's patches, and other mucosal surface-lymphoid interfaces. We describe here a previously unrecognized cathelicidin gene in chickens, chCATH-B1 , that is expressed exclusively in the epithelium of the bursa of Fabricius. Like the mature peptides of previously identified cathelicidins, the carboxyl-terminal peptide of chCATH-B1 has broad antimicrobial activity against Gram-positive and Gram-negative bacteria. chCATH-B1 expression is restricted to the secretory epithelial cell neighbors of the M cells, whereas its mature peptide is transported to become concentrated on the fibrillar network surrounding basolateral surfaces of the M cells that overlie the bursal lymphoid follicles. We conclude that chCATH-B1 is well placed to serve a protective antimicrobial role at the M cell gateway. antimicrobial peptides follicle-associated epithelium innate immunity bursa of Fabricius
Mucosal epithelial M cells provide an efficient portal of entry for microorganisms. Initially defined by their irregular microvilli and abundant transcytotic channels in the avian bursa of Fabricius, M cells also are found in the lymphoid follicle-associated epithelium of the mammalian appendix, Peyer's patches, and other mucosal surface-lymphoid interfaces. We describe here a previously unrecognized cathelicidin gene in chickens, chCATH-B1 , that is expressed exclusively in the epithelium of the bursa of Fabricius. Like the mature peptides of previously identified cathelicidins, the carboxyl-terminal peptide of chCATH-B1 has broad antimicrobial activity against Gram-positive and Gram-negative bacteria. chCATH-B1 expression is restricted to the secretory epithelial cell neighbors of the M cells, whereas its mature peptide is transported to become concentrated on the fibrillar network surrounding basolateral surfaces of the M cells that overlie the bursal lymphoid follicles. We conclude that chCATH-B1 is well placed to serve a protective antimicrobial role at the M cell gateway.
Mucosal epithelial M cells provide an efficient portal of entry for microorganisms. Initially defined by their irregular microvilli and abundant transcytotic channels in the avian bursa of Fabricius, M cells also are found in the lymphoid follicle-associated epithelium of the mammalian appendix, Peyer's patches, and other mucosal surface-lymphoid interfaces. We describe here a previously unrecognized cathelicidin gene in chickens, chCATH-B1, that is expressed exclusively in the epithelium of the bursa of Fabricius. Like the mature peptides of previously identified cathelicidins, the carboxyl-terminal peptide of chCATH-B1 has broad antimicrobial activity against Gram-positive and Gram-negative bacteria. chCATH-B1 expression is restricted to the secretory epithelial cell neighbors of the M cells, whereas its mature peptide is transported to become concentrated on the fibrillar network surrounding basolateral surfaces of the M cells that overlie the bursal lymphoid follicles. We conclude that chCATH-B1 is well placed to serve a protective antimicrobial role at the M cell gateway.
Author Cooper, Max D
Asano, Yusuke
Benyon, Lesley
Chen, Chen-lo H
Kitamura, Daisuke
Goitsuka, Ryo
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Author contributions: R.G., C.-l.H.C., and M.D.C. designed research; R.G., C.-l.H.C., L.B., and Y.A. performed research; C.-l.H.C. contributed new reagents/analytic tools; R.G., C.-l.H.C., D.K., and M.D.C. analyzed data; and R.G., C.-l.H.C., and M.D.C. wrote the paper.
Contributed by Max D. Cooper, July 26, 2007
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Snippet Mucosal epithelial M cells provide an efficient portal of entry for microorganisms. Initially defined by their irregular microvilli and abundant transcytotic...
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SubjectTerms Amino Acid Sequence
Amino acids
Animals
antibacterial properties
Antimicrobial Cationic Peptides - genetics
Antimicrobial Cationic Peptides - pharmacology
Antimicrobial Cationic Peptides - physiology
antimicrobial peptides
Antimicrobials
Avian Proteins - genetics
Avian Proteins - pharmacology
Avian Proteins - physiology
B lymphocytes
bacterial infections
Base Sequence
Biological Sciences
bursa of Fabricius
Bursa of Fabricius - cytology
Bursa of Fabricius - immunology
cathelicidin-B1
Cells
Cellular immunity
Chickens
Chickens - immunology
Complementary DNA
disease resistance
DNA, Complementary - metabolism
Epithelial cells
Epithelial Cells - immunology
epithelium
exons
gene expression
Genes
Gram-negative bacteria
Gram-Negative Bacteria - drug effects
Gram-positive bacteria
Gram-Positive Bacteria - drug effects
Immune system
Immunity, Mucosal
Immunohistochemistry
messenger RNA
Molecular Sequence Data
mucosa
nucleotide sequences
Peptides
Phylogeny
Poultry
Proteins
Skin
T lymphocytes
Title Chicken cathelicidin-B1, an antimicrobial guardian at the mucosal M cell gateway
URI https://www.jstor.org/stable/25449084
http://www.pnas.org/content/104/38/15063.abstract
https://www.ncbi.nlm.nih.gov/pubmed/17827276
https://www.proquest.com/docview/201431840
https://search.proquest.com/docview/19791326
https://search.proquest.com/docview/68288841
https://pubmed.ncbi.nlm.nih.gov/PMC1986613
Volume 104
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