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]. 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[3].
Structural highlights (PDB ID 4f8p)[4]
- . Water molecules are shown as red spheres.
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3D Structures of adhesin3D Structures of adhesin
Updated on 20-December-2018
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- Fimbrial adhesin
- 4k0o, 2bs8, 2bsc, 2bsb, 5nwp – EcF17b-G lectin domain – Escherichia coli
- 1o9z, 1o9w, 1o9v – EcF17a-G lectin domain
- 5vq5 – EcF17 lectin domain (mutant)
- 1oio – EcF17c lectin domain
- 4b4p, 4bwo – EcF18 lectin domain
- 4auu, 1uwf, 1tr7, 5fwr – EcAdh FimH lectin domain
- 5mca, 5fx3 – EcAdh FimH lectin domain (mutant)
- 5afo – EcAdh LF82
- 6aow – EcAdh FMLH lectin domain
- 3zk7 – SpPsaA - Streptococcus pneumoniae
- 3zk8, 3zk9, 3zka – SpPsaA (mutant)
- 3u4k – Adh lectin domain – Klebsiella pneumoniae
- Fimbrial adhesion complexes
- 4b4q, 4b4r – EcF18 lectin domain + hexasaccharide
- 4w6w, 4w6x, 4w6y – EcF18 lectin domain + nanobody
- 4j3o – EcAdh FimH + FimG + FimC + FimF + FimD
- 3rfz, 1ze3 – EcAdh FimH + FimC + FimD
- 1qun, 1klf, 1kiu – EcAdh FimH + FimC
- 4xo9 – EcAdh FimH + DSG residues 24-37
- 4xod, 4xoa – EcAdh FimH + FimG residues 24-37
- 4xob – EcAdh FimH + FimF residues 24-37 + mannoside derivative
- 5jr4, 5jqi – EcAdh FimH (mutant) + FimG N-terminal
- 6as8, 6arm, 6aoy – EcAdh FMLD lectin domain + galactoside derivative
- 6aox – EcAdh FMLD lectin domain + TF antigen
- 6aro – EcAdh FMLH lectin domain + quinoline derivative
- 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 – EcAdh FimH lectin domain + mannoside derivative
- 5cgb – EcAdh FimH lectin domain + galactitol
- 5ab1, 4x50 – EcAdh FimH + mannoside derivative
- 5aap, 5aal, 5mts – EcAdh FimH lectin domain + anti-adhesive
- 3f6j, 3f64, 1zpl, 1zk5 – EcF17a-G lectin domain + GlcNAc derivative
- 1psz – SpPsaA + Zn – Streptococcus pneumonia
- 3ztt – SpPsaA + Mn
- 4utp, 4uto – SpPsaA + Cd
- 2bs7 – EcF17b-G lectin domain + chitobiose
- 3ffo – EcF17b-G lectin domain + GlcNac-Man
- 4b4q, 4b4r – EcFedF lectin domain + hexasaccharide
- 4w6w, 4w6x, 4w6y – EcFedF lectin domain + nanobody
- 4f8l – YpPsaA + galactose + inhibitor – Yersinia pestis
- 4f8n – YpPsaA + galactose + phosphate choline
- 4f8o – YpPsaA + lactose + inhibitor
- 4f8p – YpPsaA + galactose
- Epitheial adhesin
- 4d3w, 4asl, 4af9 – CgAdh epithelial 1 A domain – Candida glabrata
- 4afc, 4afb, 4afa – CgAdh epithelial 1 A domain (mutant)
- 4cp2, 4cp1, 4cp0 – CgAdh epithelial 9 A domain
- 4coz, 4coy, 4cow, 4cov, 4cou – CgAdh epithelial 6 A domain
- Collagen adhesin (CAdh)
- 1amx – SaCAdh CBD – Staphylococcus aureus
- 1d2o – SaCAdh B1 repeat unit
- 1d2p – SaCAdh B1-B2 repeat units
- 2f68 – SaCAdh extracellular domain
- 2f6a – SaCAdh extracellular domain + collagen
- 2okm, 2z1p – CAdh CBD – Enterococcus faecalis
- 1p9h – YeYadA CBD – Yersinia enterocolitica
- 3h7x – YeYadA stalk domain
- 3h7z – YeYadA stalk domain (mutant)
- 3lt6, 3lt7 – YeYadA coiled coil
- 2lme – YeYadA coiled coil - NMR
- Serine-rich adhesin for platelets (SRAP)
- 4m00 – SaSRAP LBD
- 4m01 – SaSRAP LBD N-terminal
- 4m02 – SaSRAP LBD middle region
- 4m03 – SaSRAP LBD C-terminal
- Adhesin
- 2odl, 2gr8, 2gr7 – HiAdh secretion domain – Haemophilus influenzae
- 3emf – HiAdh residues 51-166
- 3emi – HiAdh residues 307-422 (mutant)
- 1s7m – HiAdh residues 548-706
- 3emo – HiAdh residues 937-1098
- 4zh7, 4zh0 – Adh BABA – Helicobacter pylori
- 4usx – Adh trimeric autotransporter – Burkholderia pseudomallei
- 3wqa, 3wpr, 3wpp, 3wpo, 3wpa – AcAdh trimeric autotransporter C-terminal – Acinetobacter
- 3wp8 – AcAdh trimeric autotransporter C-terminal (mutant)
- 4err – Adh autotransporter effector domain – Vibrio vulnificus
- 2wps, 2wpr, 2wpq – Adh trimeric autotransporter residues 483-523 – Salmonella enterica
- 4tsh – Adh surface protein – Streptococcus mutans
- 4mee – EcAdh diffuse adherence C-terminal
- 5lvy – EcAdh lectin domain
- 3etw – FnAdh A – Fusobacterium nucleatum
- 3etz, 3ety, 3etx, 2gl2 – FnAdh A (mutant)
- 3d9x – Adh A – Bartonella henselae
- 2lwb – Adh WI-1 – Ajellomyces dermatitidis
- 5my7 – Adh – Neisseria meningitidis
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
- ↑ 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
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