Linked Life Data

16845633

Source:http://linkedlifedata.com/resource/pubmed/id/16845633

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2006-7-17
pubmed:abstractText
Moraxella catarrhalis is one of the leading causes of exacerbations in chronic obstructive pulmonary disease (COPD). In the present article, we show that moraxella (n=15) binds to the major basement-membrane glycoprotein laminin, which is thickened in the airways of smokers. Using clinical strains of M. catarrhalis and their corresponding ubiquitous surface protein (Usp) A1/A2 mutants, we demonstrate that UspA1 and UspA2 are important for the laminin interaction. Binding assays with recombinant proteins demonstrated that the binding regions are localized within the N-terminal fragments, where both proteins form a globular head. Thus, UspA1/A2-dependent interactions with laminin might promote bacterial adhesion, particularly in smokers with COPD.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0022-1899
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
194
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
493-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
The respiratory pathogen moraxella catarrhalis binds to laminin via ubiquitous surface proteins A1 and A2.
pubmed:affiliation
Medical Microbiology, Department of Laboratory Medicine, Malmo University Hospital, Lund University, SE-205 02 Malmo, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Evaluation Studies