Structure of the head of the Bartonella adhesin BadA.

Trimeric autotransporter adhesins (TAAs) are a major class of proteins by which pathogenic proteobacteria adhere to their hosts. Prominent examples include Yersinia YadA, Haemophilus Hia and Hsf, Moraxella UspA1 and A2, and Neisseria NadA. TAAs also occur in symbiotic and environmental species and p...

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Autores principales:	Pawel Szczesny, Dirk Linke, Astrid Ursinus, Kerstin Bär, Heinz Schwarz, Tanja M Riess, Volkhard A J Kempf, Andrei N Lupas, Jörg Martin, Kornelius Zeth
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2008
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/bfe5bc0db5984d03a3ef307430abe2e1
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spelling	oai:doaj.org-article:bfe5bc0db5984d03a3ef307430abe2e12021-11-25T05:46:28ZStructure of the head of the Bartonella adhesin BadA.1553-73661553-737410.1371/journal.ppat.1000119https://doaj.org/article/bfe5bc0db5984d03a3ef307430abe2e12008-08-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/18688279/pdf/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374Trimeric autotransporter adhesins (TAAs) are a major class of proteins by which pathogenic proteobacteria adhere to their hosts. Prominent examples include Yersinia YadA, Haemophilus Hia and Hsf, Moraxella UspA1 and A2, and Neisseria NadA. TAAs also occur in symbiotic and environmental species and presumably represent a general solution to the problem of adhesion in proteobacteria. The general structure of TAAs follows a head-stalk-anchor architecture, where the heads are the primary mediators of attachment and autoagglutination. In the major adhesin of Bartonella henselae, BadA, the head consists of three domains, the N-terminal of which shows strong sequence similarity to the head of Yersinia YadA. The two other domains were not recognizably similar to any protein of known structure. We therefore determined their crystal structure to a resolution of 1.1 A. Both domains are beta-prisms, the N-terminal one formed by interleaved, five-stranded beta-meanders parallel to the trimer axis and the C-terminal one by five-stranded beta-meanders orthogonal to the axis. Despite the absence of statistically significant sequence similarity, the two domains are structurally similar to domains from Haemophilus Hia, albeit in permuted order. Thus, the BadA head appears to be a chimera of domains seen in two other TAAs, YadA and Hia, highlighting the combinatorial evolutionary strategy taken by pathogens.Pawel SzczesnyDirk LinkeAstrid UrsinusKerstin BärHeinz SchwarzTanja M RiessVolkhard A J KempfAndrei N LupasJörg MartinKornelius ZethPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 4, Iss 8, p e1000119 (2008)
institution	DOAJ
collection	DOAJ
language	EN
topic	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
spellingShingle	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 Pawel Szczesny Dirk Linke Astrid Ursinus Kerstin Bär Heinz Schwarz Tanja M Riess Volkhard A J Kempf Andrei N Lupas Jörg Martin Kornelius Zeth Structure of the head of the Bartonella adhesin BadA.
description	Trimeric autotransporter adhesins (TAAs) are a major class of proteins by which pathogenic proteobacteria adhere to their hosts. Prominent examples include Yersinia YadA, Haemophilus Hia and Hsf, Moraxella UspA1 and A2, and Neisseria NadA. TAAs also occur in symbiotic and environmental species and presumably represent a general solution to the problem of adhesion in proteobacteria. The general structure of TAAs follows a head-stalk-anchor architecture, where the heads are the primary mediators of attachment and autoagglutination. In the major adhesin of Bartonella henselae, BadA, the head consists of three domains, the N-terminal of which shows strong sequence similarity to the head of Yersinia YadA. The two other domains were not recognizably similar to any protein of known structure. We therefore determined their crystal structure to a resolution of 1.1 A. Both domains are beta-prisms, the N-terminal one formed by interleaved, five-stranded beta-meanders parallel to the trimer axis and the C-terminal one by five-stranded beta-meanders orthogonal to the axis. Despite the absence of statistically significant sequence similarity, the two domains are structurally similar to domains from Haemophilus Hia, albeit in permuted order. Thus, the BadA head appears to be a chimera of domains seen in two other TAAs, YadA and Hia, highlighting the combinatorial evolutionary strategy taken by pathogens.
format	article
author	Pawel Szczesny Dirk Linke Astrid Ursinus Kerstin Bär Heinz Schwarz Tanja M Riess Volkhard A J Kempf Andrei N Lupas Jörg Martin Kornelius Zeth
author_facet	Pawel Szczesny Dirk Linke Astrid Ursinus Kerstin Bär Heinz Schwarz Tanja M Riess Volkhard A J Kempf Andrei N Lupas Jörg Martin Kornelius Zeth
author_sort	Pawel Szczesny
title	Structure of the head of the Bartonella adhesin BadA.
title_short	Structure of the head of the Bartonella adhesin BadA.
title_full	Structure of the head of the Bartonella adhesin BadA.
title_fullStr	Structure of the head of the Bartonella adhesin BadA.
title_full_unstemmed	Structure of the head of the Bartonella adhesin BadA.
title_sort	structure of the head of the bartonella adhesin bada.
publisher	Public Library of Science (PLoS)
publishDate	2008
url	https://doaj.org/article/bfe5bc0db5984d03a3ef307430abe2e1
work_keys_str_mv	AT pawelszczesny structureoftheheadofthebartonellaadhesinbada AT dirklinke structureoftheheadofthebartonellaadhesinbada AT astridursinus structureoftheheadofthebartonellaadhesinbada AT kerstinbar structureoftheheadofthebartonellaadhesinbada AT heinzschwarz structureoftheheadofthebartonellaadhesinbada AT tanjamriess structureoftheheadofthebartonellaadhesinbada AT volkhardajkempf structureoftheheadofthebartonellaadhesinbada AT andreinlupas structureoftheheadofthebartonellaadhesinbada AT jorgmartin structureoftheheadofthebartonellaadhesinbada AT korneliuszeth structureoftheheadofthebartonellaadhesinbada
_version_	1718414481331060736

Structure of the head of the Bartonella adhesin BadA.

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