Adhesin
From Proteopedia
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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>. For trimeric autotransporter adhesin see [[EibD]]. | + | '''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''' or '''Mgp-operon protein 3''' and '''P140'''<ref>PMID:30367053</ref>. See also [[Journal:Acta Cryst D:S2059798320008116|Novel structure of the N-terminal helical domain of BibA, a Group B Streptococcus immunogenic bacterial adhesin]]. |
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| + | For trimeric autotransporter adhesin see [[EibD]]. | ||
== Disease == | == Disease == | ||
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</StructureSection> | </StructureSection> | ||
| - | == 3D Structures of adhesin == | ||
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| - | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
| - | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
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| - | *Fimbrial adhesin | ||
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| - | **[[4k0o]], [[2bs8]], [[2bsc]], [[2bsb]], [[5nwp]] – EcF17b-G lectin domain – ''Escherichia coli'' <BR /> | ||
| - | **[[1o9z]], [[1o9w]], [[1o9v]] – EcF17a-G lectin domain <BR /> | ||
| - | **[[5vq5]] – EcF17 lectin domain (mutant) <BR /> | ||
| - | **[[1oio]] – EcF17c lectin domain <BR /> | ||
| - | **[[4b4p]], [[4bwo]] – EcF18 lectin domain <BR /> | ||
| - | **[[4auu]], [[1uwf]], [[1tr7]], [[5fwr]] – EcAdh FimH lectin domain <BR /> | ||
| - | **[[5mca]], [[5fx3]], [[5fs5]] – EcAdh FimH lectin domain (mutant) <BR /> | ||
| - | **[[5afo]] – EcAdh LF82 <BR /> | ||
| - | **[[6aow]] – EcAdh FMLH lectin domain <BR /> | ||
| - | **[[3zk7]] – SpPsaA - ''Streptococcus pneumoniae'' <br /> | ||
| - | **[[3zk8]], [[3zk9]], [[3zka]] – SpPsaA (mutant)<br /> | ||
| - | **[[3u4k]] – Adh lectin domain – ''Klebsiella pneumoniae''<BR /> | ||
| - | **[[6h1q]] – Adh – ''Proteus mirabilis'' <br /> | ||
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| - | *Fimbrial adhesion complexes | ||
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| - | **[[4b4q]], [[4b4r]] – EcF18 lectin domain + hexasaccharide <BR /> | ||
| - | **[[4w6w]], [[4w6x]], [[4w6y]] – EcF18 lectin domain + nanobody <BR /> | ||
| - | **[[4j3o]] – EcAdh FimH + FimG + FimC + FimF + FimD <BR /> | ||
| - | **[[6e14]], [[6e15]] – EcAdh FimH + FimG + FimC + FimF + FimD - Cryo EM<BR /> | ||
| - | **[[3rfz]], [[1ze3]] – EcAdh FimH + FimC + FimD <BR /> | ||
| - | **[[1qun]], [[1klf]], [[1kiu]] – EcAdh FimH + FimC <BR /> | ||
| - | **[[4xo9]] – EcAdh FimH + DSG residues 24-37 <BR /> | ||
| - | **[[4xod]], [[4xoa]] – EcAdh FimH + FimG residues 24-37 <BR /> | ||
| - | **[[4xob]] – EcAdh FimH + FimF residues 24-37 + mannoside derivative<BR /> | ||
| - | **[[5jr4]], [[5jqi]] – EcAdh FimH (mutant) + FimG N-terminal <BR /> | ||
| - | **[[6as8]], [[6arm]], [[6aoy]] – EcAdh FMLD lectin domain + galactoside derivative <BR /> | ||
| - | **[[6aox]] – EcAdh FMLD lectin domain + TF antigen <BR /> | ||
| - | **[[6aro]] – EcAdh FMLH lectin domain + quinoline derivative <BR /> | ||
| - | **[[5muc]], [[5l4y]], [[5l4x]], [[5l4w]], [[5l4v]], [[5l4u]], [[5l4t]], [[5jcq]], [[5jcr]], [[5f2f]], [[5f3f]], [[5abz]], [[4xo8]], [[4x5p]], [[4x5q]], [[4x5r]], [[4lov]], [[4css]], [[4cst]], [[4att]], [[4auj]], [[4auy]], [[4av0]], [[4av4]], [[4av5]], [[4avh]], [[4avi]], [[4avj]], [[4avk]], [[3zl1]], [[3zl2]], [[2vco]], [[6gtx]], [[6gty]] – EcAdh FimH lectin domain + mannoside derivative <BR /> | ||
| - | **[[5cgb]] – EcAdh FimH lectin domain + galactitol <BR /> | ||
| - | **[[5ab1]], [[4x50]] – EcAdh FimH + mannoside derivative <BR /> | ||
| - | **[[5aap]], [[5aal]], [[5mts]] – EcAdh FimH lectin domain + anti-adhesive <BR /> | ||
| - | **[[3f6j]], [[3f64]], [[1zpl]], [[1zk5]] – EcF17a-G lectin domain + GlcNAc derivative <BR /> | ||
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| - | **[[1psz]] – SpPsaA + Zn – ''Streptococcus pneumonia''<br /> | ||
| - | **[[3ztt]] – SpPsaA + Mn<br /> | ||
| - | **[[4utp]], [[4uto]] – SpPsaA + Cd<br /> | ||
| - | **[[2bs7]] – EcF17b-G lectin domain + chitobiose <BR /> | ||
| - | **[[3ffo]] – EcF17b-G lectin domain + GlcNac-Man <BR /> | ||
| - | **[[4b4q]], [[4b4r]] – EcFedF lectin domain + hexasaccharide <BR /> | ||
| - | **[[4w6w]], [[4w6x]], [[4w6y]] – EcFedF lectin domain + nanobody <BR /> | ||
| - | **[[4f8l]] – YpPsaA + galactose + inhibitor – ''Yersinia pestis'' <BR /> | ||
| - | **[[4f8n]] – YpPsaA + galactose + phosphate choline <BR /> | ||
| - | **[[4f8o]] – YpPsaA + lactose + inhibitor <BR /> | ||
| - | **[[4f8p]] – YpPsaA + galactose <BR /> | ||
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| - | *Epitheial adhesin | ||
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| - | **[[4d3w]], [[4asl]], [[4af9]] – CgAdh epithelial 1 A domain – ''Candida glabrata''<br /> | ||
| - | **[[4afc]], [[4afb]], [[4afa]] – CgAdh epithelial 1 A domain (mutant)<br /> | ||
| - | **[[4cp2]], [[4cp1]], [[4cp0]] – CgAdh epithelial 9 A domain <br /> | ||
| - | **[[4coz]], [[4coy]], [[4cow]], [[4cov]], [[4cou]] – CgAdh epithelial 6 A domain <br /> | ||
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| - | *Collagen adhesin (CAdh) | ||
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| - | **[[1amx]] – SaCAdh CBD – ''Staphylococcus aureus''<br /> | ||
| - | **[[1d2o]] – SaCAdh B1 repeat unit<br /> | ||
| - | **[[1d2p]] – SaCAdh B1-B2 repeat units<br /> | ||
| - | **[[2f68]] – SaCAdh extracellular domain<br /> | ||
| - | **[[2f6a]] – SaCAdh extracellular domain + collagen<br /> | ||
| - | **[[2okm]], [[2z1p]] – CAdh CBD – ''Enterococcus faecalis''<br /> | ||
| - | **[[1p9h]] – YeYadA CBD – ''Yersinia enterocolitica''<br /> | ||
| - | **[[3h7x]] – YeYadA stalk domain<br /> | ||
| - | **[[3h7z]] – YeYadA stalk domain (mutant)<br /> | ||
| - | **[[3lt6]], [[3lt7]] – YeYadA coiled coil<br /> | ||
| - | **[[2lme]] – YeYadA coiled coil - NMR<br /> | ||
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| - | *Serine-rich adhesin for platelets (SRAP) | ||
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| - | **[[4m00]] – SaSRAP LBD<br /> | ||
| - | **[[4m01]] – SaSRAP LBD N-terminal<br /> | ||
| - | **[[4m02]] – SaSRAP LBD middle region<br /> | ||
| - | **[[4m03]] – SaSRAP LBD C-terminal<br /> | ||
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| - | *Adhesin | ||
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| - | **[[2odl]], [[2gr8]], [[2gr7]] – HiAdh secretion domain – ''Haemophilus influenzae''<br /> | ||
| - | **[[3emf]] – HiAdh residues 51-166<br /> | ||
| - | **[[3emi]] – HiAdh residues 307-422 (mutant)<br /> | ||
| - | **[[1s7m]] – HiAdh residues 548-706<br /> | ||
| - | **[[3emo]] – HiAdh residues 937-1098<br /> | ||
| - | **[[4zh7]], [[4zh0]] – Adh BABA – ''Helicobacter pylori''<br /> | ||
| - | **[[4usx]] – Adh trimeric autotransporter – ''Burkholderia pseudomallei''<br /> | ||
| - | **[[3wqa]], [[3wpr]], [[3wpp]], [[3wpo]], [[3wpa]] – AcAdh trimeric autotransporter C-terminal – ''Acinetobacter''<br /> | ||
| - | **[[3wp8]] – AcAdh trimeric autotransporter C-terminal (mutant)<br /> | ||
| - | **[[4err]] – Adh autotransporter effector domain – ''Vibrio vulnificus''<br /> | ||
| - | **[[2wps]], [[2wpr]], [[2wpq]] – Adh trimeric autotransporter residues 483-523 – ''Salmonella enterica''<br /> | ||
| - | **[[4tsh]] – Adh surface protein – ''Streptococcus mutans''<br /> | ||
| - | **[[4mee]] – EcAdh diffuse adherence C-terminal <br /> | ||
| - | **[[5lvy]] – EcAdh lectin domain <BR /> | ||
| - | **[[3etw]] – FnAdh A – ''Fusobacterium nucleatum'' <BR /> | ||
| - | **[[3etz]], [[3ety]], [[3etx]], [[2gl2]] – FnAdh A (mutant) <BR /> | ||
| - | **[[3d9x]] – Adh A – ''Bartonella henselae'' <BR /> | ||
| - | **[[2lwb]] – Adh WI-1 – ''Ajellomyces dermatitidis'' <BR /> | ||
| - | **[[5my7]] – NmAdh residues 1-124 – ''Neisseria meningitidis'' <BR /> | ||
| - | **[[6eun]] – NmAdh residues 24-170<BR /> | ||
| - | **[[6eup]] – NmAdh residues 24-170 (mutant)<BR /> | ||
| - | **[[6gq4]] – Adh residues 83-185 – ''Neisseria gonorheae''<BR /> | ||
| - | }} | ||
Current revision
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References
- ↑ 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
