Adhesin: Difference between revisions
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== Function == | == Function == | ||
'''Adhesins''' (Adh) are surface components of bacteria which facillitate adhesion to surfaces or other cells. Adh are specific surface recognition protein and are regarded as virulence factors.<ref>PMID:11043979</ref> '''FimH''' is the ''E. coli'' adhesin which is part of the type 1 pili of the bacteria. The pili is composed of subunits '''FimF, FimG''' and '''FimD'''<ref>PMID:18369105</ref>. | '''Adhesins''' (Adh) are surface components of bacteria which facillitate adhesion to surfaces or other cells. Adh are specific surface recognition protein and are regarded as virulence factors.<ref>PMID:11043979</ref> '''FimH''' is the ''E. coli'' adhesin which is part of the type 1 pili of the bacteria. The pili is composed of subunits '''FimF, FimG''' and '''FimD'''<ref>PMID:18369105</ref>. The main Adhesins of the pathogen ''Mycoplasma genitalium'' are '''P110''' and '''P140'''<ref>PMID:30367053</ref>. | ||
For trimeric autotransporter adhesin see [[EibD]]. | For trimeric autotransporter adhesin see [[EibD]]. | ||
Revision as of 11:47, 9 March 2021
FunctionAdhesins (Adh) are surface components of bacteria which facillitate adhesion to surfaces or other cells. Adh are specific surface recognition protein and are regarded as virulence factors.[1] FimH is the E. coli adhesin which is part of the type 1 pili of the bacteria. The pili is composed of subunits FimF, FimG and FimD[2]. The main Adhesins of the pathogen Mycoplasma genitalium are P110 and P140[3]. For trimeric autotransporter adhesin see EibD. DiseaseBacterial pathogens use adhesins as a major factor in adhesion-based virulence. Adhesins serve as vaccine targets since they are essential to infection[4]. Structural highlights
3D Structures of adhesin
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ReferencesReferences
- ↑ Klemm P, Schembri MA. Bacterial adhesins: function and structure. Int J Med Microbiol. 2000 Mar;290(1):27-35. PMID:11043979 doi:http://dx.doi.org/10.1016/S1438-4221(00)80102-2
- ↑ Nishiyama M, Ishikawa T, Rechsteiner H, Glockshuber R. Reconstitution of pilus assembly reveals a bacterial outer membrane catalyst. Science. 2008 Apr 18;320(5874):376-9. doi: 10.1126/science.1154994. Epub 2008 Mar, 27. PMID:18369105 doi:http://dx.doi.org/10.1126/science.1154994
- ↑ Aparicio D, Torres-Puig S, Ratera M, Querol E, Pinol J, Pich OQ, Fita I. Mycoplasma genitalium adhesin P110 binds sialic-acid human receptors. Nat Commun. 2018 Oct 26;9(1):4471. doi: 10.1038/s41467-018-06963-y. PMID:30367053 doi:http://dx.doi.org/10.1038/s41467-018-06963-y
- ↑ Wizemann TM, Adamou JE, Langermann S. Adhesins as targets for vaccine development. Emerg Infect Dis. 1999 May-Jun;5(3):395-403. doi: 10.3201/eid0503.990310. PMID:10341176 doi:http://dx.doi.org/10.3201/eid0503.990310
- ↑ Bao R, Nair MK, Tang WK, Esser L, Sadhukhan A, Holland RL, Xia D, Schifferli DM. Structural basis for the specific recognition of dual receptors by the homopolymeric pH 6 antigen (Psa) fimbriae of Yersinia pestis. Proc Natl Acad Sci U S A. 2013 Jan 15;110(3):1065-70. doi:, 10.1073/pnas.1212431110. Epub 2012 Dec 31. PMID:23277582 doi:10.1073/pnas.1212431110