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. 1989 Apr;57(4):1285–1289. doi: 10.1128/iai.57.4.1285-1289.1989

Sialo-oligosaccharide receptors for Mycoplasma pneumoniae and related oligosaccharides of poly-N-acetyllactosamine series are polarized at the cilia and apical-microvillar domains of the ciliated cells in human bronchial epithelium.

R W Loveless 1, T Feizi 1
PMCID: PMC313263  PMID: 2494113

Abstract

The occurrence and distribution of the sialo-oligosaccharide receptors (sialosyl-I and sialosyl-i) for Mycoplasma pneumoniae as well as other related oligosaccharide structures of poly-N-acetyllactosamine type, and their short-chain analogs based on galactose linked beta 1-4 or beta 1-3 to N-acetylglucosamine (Gal beta 1-4GlcNAc or Gal beta 1-3GlcNAc, respectively) were investigated in the human bronchial epithelium by histochemistry by using sequence-specific monoclonal antibodies and lectins. Among the mature epithelial cells, only ciliated cells were found to express the long-chain antigens, whereas mucus-secreting cells contained the short-chain antigens associated with mucus globules. The long-chain oligosaccharides were found to be highly polarized at the luminal aspects of the ciliated cells where the branched structures (I and sialosyl-I antigens) were detected both at the apical-microvillar border and on the cilia, but the linear structures (i, sialosyl-i, and VIM-2 antigens) were detected exclusively at the apical-microvillar border. These observations provide the first in situ visualization of the receptor structures for M. pneumoniae at the primary site of infection. The lack of sialo-oligosaccharide receptors in secretory cells and the mucus they produce provides a biochemical basis for evasion by this microorganism of the secreted mucus barrier.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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