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Haemophilus influen...
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Singh, BirendraLund University,Lunds universitet,Medicinsk mikrobiologi,Forskargrupper vid Lunds universitet,Medical Microbiology,Lund University Research Groups
(author)
Haemophilus influenzae surface fibril (Hsf) is a unique twisted hairpin-like trimeric autotransporter
- Article/chapterEnglish2015
Publisher, publication year, extent ...
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Elsevier BV,2015
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11 s.
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electronicrdacarrier
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LIBRIS-ID:oai:lup.lub.lu.se:f93a715d-cb14-442d-bfa8-539bfc8a8846
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https://lup.lub.lu.se/record/4912873URI
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https://doi.org/10.1016/j.ijmm.2014.10.004DOI
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Language:English
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Summary in:English
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Subject category:art swepub-publicationtype
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Subject category:ref swepub-contenttype
Notes
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The Haemophilus surface fibril (Hsf) is an extraordinary large (2413 amino acids) trimeric autotransporter, present in all encapsulated Haemophilus influenzae. It contributes to virulence by directly functioning as an adhesin. Furthermore, Hsf recruits the host factor vitronectin thereby inhibiting the host innate immune response resulting in enhanced survival in serum. Here we observed by electron microscopy that Hsf appears as an 100. nm long fibril at the bacterial surface albeit the length is approximately 200. nm according to a bioinformatics based model. To unveil this discrepancy, we denaturated Hsf at the surface of Hib by using guanidine hydrochloride (GuHCl). Partial denaturation induced in the presence of GuHCl unfolded the Hsf molecules, and resulted in an increased length of fibres in comparison to the native trimeric form. Importantly, our findings were also verified by E. coli expressing Hsf at its surface. In addition, a set of Hsf-specific peptide antibodies also indicated that the N-terminal of Hsf is located near the C-terminal at the base of the fibril. Taken together, our results demonstrated that Hsf is not a straight molecule but is folded and doubled over. This is the first report that provides the unique structural features of the trimeric autotransporter Hsf.
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Jubair, Tamim AlLund University,Lunds universitet,Medicinsk mikrobiologi,Forskargrupper vid Lunds universitet,Medical Microbiology,Lund University Research Groups(Swepub:lu)med-tmj
(author)
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Mörgelin, MatthiasLund University,Lunds universitet,Infektionsmedicin,Sektion III,Institutionen för kliniska vetenskaper, Lund,Medicinska fakulteten,Infection Medicine (BMC),Section III,Department of Clinical Sciences, Lund,Faculty of Medicine(Swepub:lu)medk-mmn
(author)
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Sundin, AndersLund University,Lunds universitet,Centrum för analys och syntes,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Centre for Analysis and Synthesis,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH(Swepub:lu)ok2-aps
(author)
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Linse, SaraLund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH(Swepub:lu)fkm2-sli
(author)
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Nilsson, Ulf J.Lund University,Lunds universitet,Centrum för analys och syntes,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Centre for Analysis and Synthesis,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH(Swepub:lu)ok2-uni
(author)
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Riesbeck, KristianLund University,Lunds universitet,Medicinsk mikrobiologi,Forskargrupper vid Lunds universitet,Medical Microbiology,Lund University Research Groups(Swepub:lu)mikr-kri
(author)
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Medicinsk mikrobiologiForskargrupper vid Lunds universitet
(creator_code:org_t)
Related titles
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In:International Journal of Medical Microbiology: Elsevier BV305:1, s. 27-371618-06071438-4221
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