"Adhesins, Bacterial" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
Cell-surface components or appendages of bacteria that facilitate adhesion (BACTERIAL ADHESION) to other cells or to inanimate surfaces. Most fimbriae (FIMBRIAE, BACTERIAL) of gram-negative bacteria function as adhesins, but in many cases it is a minor subunit protein at the tip of the fimbriae that is the actual adhesin. In gram-positive bacteria, a protein or polysaccharide surface layer serves as the specific adhesin. What is sometimes called polymeric adhesin (BIOFILMS) is distinct from protein adhesin.
| Descriptor ID |
D018829
|
| MeSH Number(s) |
D12.776.097.120.050 D12.776.543.100.050 D23.050.161.050
|
| Concept/Terms |
|
Below are MeSH descriptors whose meaning is more general than "Adhesins, Bacterial".
Below are MeSH descriptors whose meaning is more specific than "Adhesins, Bacterial".
This graph shows the total number of publications written about "Adhesins, Bacterial" by people in this website by year, and whether "Adhesins, Bacterial" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2007 | 1 | 0 | 1 |
| 2008 | 1 | 0 | 1 |
| 2010 | 1 | 0 | 1 |
| 2011 | 1 | 0 | 1 |
| 2012 | 1 | 0 | 1 |
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Below are the most recent publications written about "Adhesins, Bacterial" by people in Profiles.
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Crystal structure of JlpA, a surface-exposed lipoprotein adhesin of Campylobacter jejuni. J Struct Biol. 2012 Feb; 177(2):583-8.
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Structural insights into the glycosyltransferase activity of the Actinobacillus pleuropneumoniae HMW1C-like protein. J Biol Chem. 2011 Nov 04; 286(44):38546-38557.
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The Actinobacillus pleuropneumoniae HMW1C-like glycosyltransferase mediates N-linked glycosylation of the Haemophilus influenzae HMW1 adhesin. PLoS One. 2010 Dec 30; 5(12):e15888.
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The TpsB translocator HMW1B of haemophilus influenzae forms a large conductance channel. J Biol Chem. 2008 Jun 06; 283(23):15771-8.
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The structure of the Haemophilus influenzae HMW1 pro-piece reveals a structural domain essential for bacterial two-partner secretion. J Biol Chem. 2007 Oct 19; 282(42):31076-84.