Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Bente Børud"'
Autor:
Bente Børud, Michael Koomey
Publikováno v:
Frontiers in Cellular and Infection Microbiology, Vol 14 (2024)
The genus Neisseria, which colonizes mucosal surfaces, includes both commensal and pathogenic species that are exclusive to humans. The two pathogenic Neisseria species are closely related but cause quite different diseases, meningococcal sepsis and
Externí odkaz:
https://doaj.org/article/6093a3f768c04b6a90b266f3b27ffe15
Autor:
Guro K. Bårnes, Ola Brønstad Brynildsrud, Bente Børud, Bereket Workalemahu, Paul A. Kristiansen, Demissew Beyene, Abraham Aseffa, Dominique A. Caugant
Publikováno v:
BMC Genomics, Vol 18, Iss 1, Pp 1-14 (2017)
Abstract Background Meningococcal colonization is a prerequisite for transmission and disease, but the bacterium only very infrequently causes disease while asymptomatic carriage is common. Carriage is highly dynamic, showing a great variety across t
Externí odkaz:
https://doaj.org/article/26a7dd4f72de410699a18923597baa7a
Autor:
Lisbeth M. Næss, Ingunn S. Maugesten, Dominique A. Caugant, Afework Kassu, Abraham Aseffa, Bente Børud
Publikováno v:
Journal of Bacteriology. 205
Bacterial meningitis is a serious global health problem, and one of the major causative organisms is Neisseria meningitidis . Extensive variability in protein glycan structure and antigenicity is due to phase variation of protein glycosylation genes
Autor:
Jan Haug Anonsen, Bente Børud, Michael Koomey, William Brynildsen Reinar, Chris Hadjineophytou, Åshild Vik, Nelson Wang
Publikováno v:
Glycobiology
Glycosylation of multiple proteins via O-linkage is well documented in bacterial species of Neisseria of import to human disease. Recent studies of protein glycosylation (pgl) gene distribution established that related protein glycosylation systems o
Autor:
Ola Brønstad Brynildsrud, Dominique A. Caugant, Elisabeth Fritzsønn, Bente Børud, Guro K. Bårnes
Publikováno v:
Journal of Bacteriology
Species within the genus Neisseria display significant glycan diversity associated with the O-linked protein glycosylation (pgl) systems due to phase variation and polymorphic genes and gene content. The aim of this study was to examine in detail the
Autor:
Bente, Børud, Guro K, Bårnes, Ola Brønstad, Brynildsrud, Elisabeth, Fritzsønn, Dominique A, Caugant
Publikováno v:
Journal of bacteriology. 200(16)
The affordability of bacterial genome sequencing has provided a helpful tool for sequencing large strain collections. Bente Børud (J.
Publikováno v:
Glycobiology
O-acetylation is a common modification of bacterial glycoconjugates. By modifying oligosaccharide structure and chemistry, O-acetylation has important consequences for biotic and abiotic recognition events and thus bacterial fitness in general. Previ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::19a14be165216b876abc5a7468a6de5d
http://hdl.handle.net/11250/2565922
http://hdl.handle.net/11250/2565922
Autor:
Ellen Hanne Cohen, Jan Haug Anonsen, Anne Berit Samuelsen, Raimonda Viburiene, Bente Børud, Michael Koomey
Publikováno v:
Molecular Microbiology. 94:688-699
Summary Glycans manifest in conjunction with the broad spectrum O-linked protein glycosylation in species within the genus Neisseria display intra- and interstrain diversity. Variability in glycan structure and antigenicity are attributable to differ
Autor:
Wolfgang Egge-Jacobsen, Michael Koomey, Bente Børud, Finn Erik Aas, Åshild Vik, Jan Haug Anonsen
Publikováno v:
Infection and Immunity. 80:22-30
The zwitterionic phospho-form moieties phosphoethanolamine (PE) and phosphocholine (PC) are important components of bacterial membranes and cell surfaces. The major type IV pilus subunit protein of Neisseria gonorrhoeae , PilE, undergoes posttranslat
Autor:
Wolfgang Egge-Jacobsen, Barbara Imperiali, Meredith D. Hartley, Raimonda Viburiene, Michael Koomey, Bente Børud, Berit Smestad Paulsen
Publikováno v:
Proceedings of the National Academy of Sciences. 108:9643-9648
Although protein glycosylation systems are becoming widely recognized in bacteria, little is known about the mechanisms and evolutionary forces shaping glycan composition. Species within the genus Neisseria display remarkable glycoform variability as