A role for the fibrinogen-binding regions of streptococcal M proteins in phagocytosis resistance
(2000) In Molecular Microbiology 37(6). p.1318-1326- Abstract
- All virulent group A streptococcal isolates bind fibrinogen, a property that is closely linked to expression of type-specific antiphagocytic surface molecules designated M proteins. Here we show that although the M proteins from two different strains, M1 and M5, both bind fibrinogen with high affinity, they interact with different regions in the ligand. Moreover, mapping experiments demonstrated that the fibrinogen-binding regions in the M1 and M5 proteins are quite dissimilar at the amino acid sequence level and that they bind to different regions in the plasma protein. In spite of these differences, the fibrinogen-binding regions of M1 and M5 could both be shown to contribute to streptococcal survival in human blood, providing evidence... (More)
- All virulent group A streptococcal isolates bind fibrinogen, a property that is closely linked to expression of type-specific antiphagocytic surface molecules designated M proteins. Here we show that although the M proteins from two different strains, M1 and M5, both bind fibrinogen with high affinity, they interact with different regions in the ligand. Moreover, mapping experiments demonstrated that the fibrinogen-binding regions in the M1 and M5 proteins are quite dissimilar at the amino acid sequence level and that they bind to different regions in the plasma protein. In spite of these differences, the fibrinogen-binding regions of M1 and M5 could both be shown to contribute to streptococcal survival in human blood, providing evidence for the distinct function of a plasma protein interaction in bacterial pathogenesis. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1116932
- author
- Ringdahl, Ulrika LU ; Svensson, Henrik LU ; Kotarsky, Heike LU ; Gustafsson, Maria ; Weineisen, Maria LU and Sjöbring, Ulf LU
- organization
- publishing date
- 2000
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Molecular Microbiology
- volume
- 37
- issue
- 6
- pages
- 1318 - 1326
- publisher
- Wiley-Blackwell
- external identifiers
-
- pmid:10998165
- scopus:0033779403
- ISSN
- 1365-2958
- DOI
- 10.1046/j.1365-2958.2000.02062.x
- language
- English
- LU publication?
- yes
- id
- 09e94f69-5420-48c0-8704-88176cfeb9d3 (old id 1116932)
- date added to LUP
- 2016-04-01 12:33:06
- date last changed
- 2022-03-29 02:24:40
@article{09e94f69-5420-48c0-8704-88176cfeb9d3, abstract = {{All virulent group A streptococcal isolates bind fibrinogen, a property that is closely linked to expression of type-specific antiphagocytic surface molecules designated M proteins. Here we show that although the M proteins from two different strains, M1 and M5, both bind fibrinogen with high affinity, they interact with different regions in the ligand. Moreover, mapping experiments demonstrated that the fibrinogen-binding regions in the M1 and M5 proteins are quite dissimilar at the amino acid sequence level and that they bind to different regions in the plasma protein. In spite of these differences, the fibrinogen-binding regions of M1 and M5 could both be shown to contribute to streptococcal survival in human blood, providing evidence for the distinct function of a plasma protein interaction in bacterial pathogenesis.}}, author = {{Ringdahl, Ulrika and Svensson, Henrik and Kotarsky, Heike and Gustafsson, Maria and Weineisen, Maria and Sjöbring, Ulf}}, issn = {{1365-2958}}, language = {{eng}}, number = {{6}}, pages = {{1318--1326}}, publisher = {{Wiley-Blackwell}}, series = {{Molecular Microbiology}}, title = {{A role for the fibrinogen-binding regions of streptococcal M proteins in phagocytosis resistance}}, url = {{http://dx.doi.org/10.1046/j.1365-2958.2000.02062.x}}, doi = {{10.1046/j.1365-2958.2000.02062.x}}, volume = {{37}}, year = {{2000}}, }