Impact of sequence diversity in the Moraxella catarrhalis UspA2/UspA2H head domain on vitronectin binding and antigenic variation.
(2013) In Microbes and Infection 15(5). p.375-387- Abstract
- The nasopharyngeal pathogen Moraxella catarrhalis recruits vitronectin to subvert complement-mediated killing. Ubiquitous surface protein (UspA) 2 and its hybrid form UspA2H bind vitronectin at the highly diverse N-terminal head domain. Here we characterized the sequence diversity of the head domain in multiple M. catarrhalis clinical isolates (n = 51) with focus on binding of vitronectin. The head domain of the uspA2 genes from 40 isolates were clustered according to an N-terminal sequence motif of UspA2 (NTER2), i.e., NTER2A (55% of uspA2 variants), NTER2B (32.5%), NTER2C (5%), and finally a group without an NTER2 (7.5%). Isolates harbouring the uspA2H gene (n = 11) contained N-terminal GGG repeats. Vitronectin binding to isolates having... (More)
- The nasopharyngeal pathogen Moraxella catarrhalis recruits vitronectin to subvert complement-mediated killing. Ubiquitous surface protein (UspA) 2 and its hybrid form UspA2H bind vitronectin at the highly diverse N-terminal head domain. Here we characterized the sequence diversity of the head domain in multiple M. catarrhalis clinical isolates (n = 51) with focus on binding of vitronectin. The head domain of the uspA2 genes from 40 isolates were clustered according to an N-terminal sequence motif of UspA2 (NTER2), i.e., NTER2A (55% of uspA2 variants), NTER2B (32.5%), NTER2C (5%), and finally a group without an NTER2 (7.5%). Isolates harbouring the uspA2H gene (n = 11) contained N-terminal GGG repeats. Vitronectin binding to isolates having UspA2 did not correlate to variation in the NTER2 motifs but occurred in UspA2H containing 6 or ≥11 of GGG repeats. Analyses of recombinant UspA2/UspA2H head domains of multiple variants showed UspA2-dependent binding to the C-terminal of vitronectin. Furthermore, polyclonal anti-UspA2 antibodies revealed that the head domain of the majority of Moraxella UspA2/2H was antigenically unrelated, whereas the full length molecules were recognized. In conclusion, the head domains of UspA2/2H have extensive sequence polymorphism without losing vitronectin-binding capacity promoting a general evasion of the host immune system. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3628365
- author
- Su, Yu-Ching LU ; Hallström, Björn ; Bernhard, Sara LU ; Singh, Birendra LU and Riesbeck, Kristian LU
- organization
- publishing date
- 2013
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Microbes and Infection
- volume
- 15
- issue
- 5
- pages
- 375 - 387
- publisher
- Elsevier
- external identifiers
-
- wos:000319539000005
- pmid:23474333
- scopus:84876881711
- pmid:23474333
- ISSN
- 1769-714X
- DOI
- 10.1016/j.micinf.2013.02.004
- language
- English
- LU publication?
- yes
- id
- c1087449-d485-4f7b-b0f3-c9c24bae50b7 (old id 3628365)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/23474333?dopt=Abstract
- date added to LUP
- 2016-04-01 10:15:54
- date last changed
- 2022-04-27 20:22:24
@article{c1087449-d485-4f7b-b0f3-c9c24bae50b7, abstract = {{The nasopharyngeal pathogen Moraxella catarrhalis recruits vitronectin to subvert complement-mediated killing. Ubiquitous surface protein (UspA) 2 and its hybrid form UspA2H bind vitronectin at the highly diverse N-terminal head domain. Here we characterized the sequence diversity of the head domain in multiple M. catarrhalis clinical isolates (n = 51) with focus on binding of vitronectin. The head domain of the uspA2 genes from 40 isolates were clustered according to an N-terminal sequence motif of UspA2 (NTER2), i.e., NTER2A (55% of uspA2 variants), NTER2B (32.5%), NTER2C (5%), and finally a group without an NTER2 (7.5%). Isolates harbouring the uspA2H gene (n = 11) contained N-terminal GGG repeats. Vitronectin binding to isolates having UspA2 did not correlate to variation in the NTER2 motifs but occurred in UspA2H containing 6 or ≥11 of GGG repeats. Analyses of recombinant UspA2/UspA2H head domains of multiple variants showed UspA2-dependent binding to the C-terminal of vitronectin. Furthermore, polyclonal anti-UspA2 antibodies revealed that the head domain of the majority of Moraxella UspA2/2H was antigenically unrelated, whereas the full length molecules were recognized. In conclusion, the head domains of UspA2/2H have extensive sequence polymorphism without losing vitronectin-binding capacity promoting a general evasion of the host immune system.}}, author = {{Su, Yu-Ching and Hallström, Björn and Bernhard, Sara and Singh, Birendra and Riesbeck, Kristian}}, issn = {{1769-714X}}, language = {{eng}}, number = {{5}}, pages = {{375--387}}, publisher = {{Elsevier}}, series = {{Microbes and Infection}}, title = {{Impact of sequence diversity in the Moraxella catarrhalis UspA2/UspA2H head domain on vitronectin binding and antigenic variation.}}, url = {{http://dx.doi.org/10.1016/j.micinf.2013.02.004}}, doi = {{10.1016/j.micinf.2013.02.004}}, volume = {{15}}, year = {{2013}}, }