AFM Identifies a Protein Complex Involved in Pathogen Adhesion Which Ruptures at Three Nanonewtons-Reference-Cited by-同舟云学术

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AFM Identifies a Protein Complex Involved in Pathogen Adhesion Which Ruptures at Three Nanonewtons

Published:2021-09-01 Issue:18 Volume:21 Page:7595-7601
ISSN:1530-6984
Container-title:Nano Letters
language:en
Short-container-title:Nano Lett.

Author:

Chantraine Constance¹,Mathelié-Guinlet Marion¹^ORCID,Pietrocola Giampiero²^ORCID,Speziale Pietro²,Dufrêne Yves F.¹^ORCID

Affiliation:

1. Louvain Institute of Biomolecular Science and Technology, UCLouvain, Croix du Sud, 4-5, bte L7.07.07, B-1348 Louvain-la-Neuve, Belgium

2. Department of Molecular Medicine, Unit of Biochemistry, University of Pavia, Viale Taramelli 3/b, 27100 Pavia, Italy

Funder

Fondazione Cariplo

Fonds De La Recherche Scientifique - FNRS

H2020 European Research Council

Research Department of the Communaut?? fran??aise de Belgique

Publisher

American Chemical Society (ACS)

Subject

Mechanical Engineering,Condensed Matter Physics,General Materials Science,General Chemistry,Bioengineering

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.nanolett.1c02105

Reference50 articles.

1. Clumping factor A, von Willebrand factor-binding protein and von Willebrand factor anchorStaphylococcus aureusto the vessel wall

2. Staphylococcus aureus vWF-binding protein triggers a strong interaction between clumping factor A and host vWF

3. 150-kD von Willebrand factor binding protein extracted from human vascular subendothelium is type VI collagen.

4. Shear-induced unfolding triggers adhesion of von Willebrand factor fibers

5. von Willebrand factor. A reduced and alkylated 52/48-kDa fragment beginning at amino acid residue 449 contains the domain interacting with platelet glycoprotein Ib.

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