Adhesin

From Proteopedia

Adhesin PsaA complex with tert-butyl formate and galactose (stick model) (PDB ID 4f8p) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Disease 3 Structural highlights 4 3D Structures of adhesin 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.[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 or Mgp-operon protein 3 and P140[3]. See also Novel structure of the N-terminal helical domain of BibA, a Group B Streptococcus immunogenic bacterial adhesin. For trimeric autotransporter adhesin see EibD. Disease Bacterial 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 (PDB ID 4f8p)[5] . Water molecules are shown as red spheres. . 3D Structures of adhesin Adhesin 3D structures

References

1. ↑ 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
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
3. ↑ 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
4. ↑ 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
5. ↑ 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