Linked Life Data

21098633

Source:http://linkedlifedata.com/resource/pubmed/id/21098633

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 24
pubmed:dateCreated
2010-12-2
pubmed:abstractText
Staphylococcus aureus, which is a leading cause of hospital-acquired infections, binds via fibronectin to integrin ?5?1, a process that can promote host colonization in vivo. Integrin engagement induces actin cytoskeleton rearrangements that result in the uptake of S. aureus by non-professional phagocytic cells. Interestingly, we found that fibronectin-binding S. aureus trigger the redistribution of membrane microdomain components. In particular, ganglioside GM1 and GPI-linked proteins were recruited upon integrin ?1 engagement, and disruption of membrane microdomains blocked bacterial internalization. Several membrane-microdomain-associated proteins, such as flotillin-1 and flotillin-2, as well as caveolin, were recruited to sites of bacterial attachment. Whereas dominant-negative versions of flotillin-2 did not affect bacterial attachment or internalization, cells deficient for caveolin-1 (Cav1(-/-)) showed increased uptake of S. aureus and other Fn-binding pathogens. Recruitment of membrane microdomains to cell-associated bacteria was unaltered in Cav1(-/-) cells. However, fluorescence recovery after photobleaching (FRAP) revealed an enhanced mobility of membrane-microdomain-associated proteins in the absence of caveolin-1. Enhanced membrane microdomain mobility and increased uptake of S. aureus was repressed by expression of wild-type caveolin-1, but not caveolin-1 G83S, which harbors a point mutation in the caveolin scaffolding domain. Similarly, chemical or physical stimulation of membrane fluidity led to increased uptake of S. aureus. These results highlight a crucial role for caveolin-1 in negative regulation of membrane microdomain mobility, thereby affecting endocytosis of bacteria-engaged integrins. This process might not only limit host cell invasion by integrin-binding bacterial pathogens, but might also be physiologically relevant for integrin-mediated cell adhesion.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1477-9137
pubmed:author
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
123
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4280-91
pubmed:meshHeading
pubmed-meshheading:21098633-Amino Acid Sequence, pubmed-meshheading:21098633-Animals, pubmed-meshheading:21098633-Antigens, CD29, pubmed-meshheading:21098633-Bacterial Adhesion, pubmed-meshheading:21098633-Bacterial Proteins, pubmed-meshheading:21098633-Blood Proteins, pubmed-meshheading:21098633-Cattle, pubmed-meshheading:21098633-Caveolin 1, pubmed-meshheading:21098633-Endocytosis, pubmed-meshheading:21098633-Fibroblasts, pubmed-meshheading:21098633-Fibronectins, pubmed-meshheading:21098633-HEK293 Cells, pubmed-meshheading:21098633-Humans, pubmed-meshheading:21098633-Membrane Microdomains, pubmed-meshheading:21098633-Membrane Proteins, pubmed-meshheading:21098633-Mice, pubmed-meshheading:21098633-Molecular Sequence Data, pubmed-meshheading:21098633-Protein Transport, pubmed-meshheading:21098633-Staphylococcal Infections, pubmed-meshheading:21098633-Staphylococcus aureus, pubmed-meshheading:21098633-src-Family Kinases
pubmed:year
2010
pubmed:articleTitle
Caveolin limits membrane microdomain mobility and integrin-mediated uptake of fibronectin-binding pathogens.
pubmed:affiliation
Lehrstuhl Zellbiologie X908, Universität Konstanz, Universitätsstr. 10, 78457 Konstanz, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't