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Binding of Haemophilus influenzae to purified mucins from the human respiratory tract

Davies, J LU ; Carlstedt, I LU ; Nilsson, Anki LU ; Håkansson, Anders P LU ; Sabharwal, H; van Alphen, L; van Ham, M and Svanborg, C LU (1995) In Infection and Immunity 63(7). p.92-2485
Abstract

Mucins are high-molecular-weight glycoproteins and major constituents of the mucus layer which covers the airway surface. We have studied the interactions between bacteria, mucins, and epithelial cells from the human respiratory tract. Nontypeable strains of Haemophilus influenzae were found to bind to purified airway mucins in suspension and on solid phase. Mucins in suspension inhibited the attachment of these strains to nasopharyngeal epithelial cells, while mucin coating of the cells enhanced their binding. In contrast, strains of Streptococcus pneumoniae and encapsulated and other nontypeable H. influenzae strains failed to interact with mucins. These H. influenzae strains used other strategies for adherence to epithelial cells.... (More)

Mucins are high-molecular-weight glycoproteins and major constituents of the mucus layer which covers the airway surface. We have studied the interactions between bacteria, mucins, and epithelial cells from the human respiratory tract. Nontypeable strains of Haemophilus influenzae were found to bind to purified airway mucins in suspension and on solid phase. Mucins in suspension inhibited the attachment of these strains to nasopharyngeal epithelial cells, while mucin coating of the cells enhanced their binding. In contrast, strains of Streptococcus pneumoniae and encapsulated and other nontypeable H. influenzae strains failed to interact with mucins. These H. influenzae strains used other strategies for adherence to epithelial cells. The type b strain 770235 attached via fimbriae but also expressed a subcapsular adhesin that was detected in a capsule- and fimbria-defective mutant. Mucin pretreatment of these bacteria did not inhibit adherence, but mucin pretreatment of epithelial cells inhibited adherence, probably by shielding of the receptors for these adhesins. Non-mucin-binding nontypeable and encapsulated H. influenzae strains would, therefore, adhere only after disruption of the mucus layer and exposure of cellular receptors. Differences in tissue toxicity and invasiveness among H. influenzae strains may also be influenced by the mucin interactions of the strains.

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organization
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Contribution to journal
publication status
published
subject
keywords
Bacterial Adhesion, Epithelium, Fimbriae, Bacterial, Haemophilus influenzae, Humans, Mucins, Nasopharynx, Respiratory System, Streptococcus pneumoniae
in
Infection and Immunity
volume
63
issue
7
pages
8 pages
publisher
American Society for Microbiology
external identifiers
  • Scopus:0029044546
ISSN
0019-9567
language
English
LU publication?
yes
id
c1a29db8-0507-4e60-b60f-10d6ff4c53b9
date added to LUP
2016-05-21 11:42:19
date last changed
2016-10-23 04:43:31
@misc{c1a29db8-0507-4e60-b60f-10d6ff4c53b9,
  abstract     = {<p>Mucins are high-molecular-weight glycoproteins and major constituents of the mucus layer which covers the airway surface. We have studied the interactions between bacteria, mucins, and epithelial cells from the human respiratory tract. Nontypeable strains of Haemophilus influenzae were found to bind to purified airway mucins in suspension and on solid phase. Mucins in suspension inhibited the attachment of these strains to nasopharyngeal epithelial cells, while mucin coating of the cells enhanced their binding. In contrast, strains of Streptococcus pneumoniae and encapsulated and other nontypeable H. influenzae strains failed to interact with mucins. These H. influenzae strains used other strategies for adherence to epithelial cells. The type b strain 770235 attached via fimbriae but also expressed a subcapsular adhesin that was detected in a capsule- and fimbria-defective mutant. Mucin pretreatment of these bacteria did not inhibit adherence, but mucin pretreatment of epithelial cells inhibited adherence, probably by shielding of the receptors for these adhesins. Non-mucin-binding nontypeable and encapsulated H. influenzae strains would, therefore, adhere only after disruption of the mucus layer and exposure of cellular receptors. Differences in tissue toxicity and invasiveness among H. influenzae strains may also be influenced by the mucin interactions of the strains.</p>},
  author       = {Davies, J and Carlstedt, I and Nilsson, Anki and Håkansson, Anders P and Sabharwal, H and van Alphen, L and van Ham, M and Svanborg, C},
  issn         = {0019-9567},
  keyword      = {Bacterial Adhesion,Epithelium,Fimbriae, Bacterial,Haemophilus influenzae,Humans,Mucins,Nasopharynx,Respiratory System,Streptococcus pneumoniae},
  language     = {eng},
  number       = {7},
  pages        = {92--2485},
  publisher    = {ARRAY(0xa9d6c28)},
  series       = {Infection and Immunity},
  title        = {Binding of Haemophilus influenzae to purified mucins from the human respiratory tract},
  volume       = {63},
  year         = {1995},
}