scholarly journals Human C4b-binding Protein, Structural Basis for Interaction with Streptococcal M Protein, a Major Bacterial Virulence Factor

2005 ◽  
Vol 281 (6) ◽  
pp. 3690-3697 ◽  
Author(s):  
Huw T. Jenkins ◽  
Linda Mark ◽  
Graeme Ball ◽  
Jenny Persson ◽  
Gunnar Lindahl ◽  
...  
Keyword(s):  
Virulence Factor ◽  
Binding Protein ◽  
Protein A ◽  
Bacterial Virulence ◽  
M Protein ◽  
Structural Basis ◽  
Streptococcal M Protein ◽  
Bacterial Virulence Factor

Purification of bacterial virulence factor pertactin using high affinity ligands

2020 ◽  
Vol 164 ◽  
pp. 107760
Author(s):  
Umatheny Umatheva ◽  
Braden Sweeting ◽  
Léo Sauvaget ◽  
Nerissa Dela Rosa ◽  
John Riley ◽  
...  
Keyword(s):  
Virulence Factor ◽  
Bacterial Virulence ◽  
Affinity Ligands ◽  
High Affinity ◽  
Bacterial Virulence Factor

scholarly journals Human Immunoglobulin G Cannot Inhibit Fibrinogen Binding by the Genetically Diverse A Domain ofStaphylococcus aureusFibronectin-Binding Protein A

mSphere ◽  
2018 ◽  
Vol 3 (2) ◽  
pp. e00590-17
Author(s):  
P. Martijn den Reijer ◽  
Mehri Tavakol ◽  
Nicole Lemmens-den Toom ◽  
Dikra Allouch ◽  
Sheila Thomas ◽  
...  
Keyword(s):  
Antibody Response ◽  
Virulence Factor ◽  
Antibody Production ◽  
Immunoglobulin G ◽  
Binding Protein ◽  
Protein A ◽  
Sequence Diversity ◽  
Enzyme Linked Immunosorbent Assay ◽  
Human Antibody ◽  
Fibrinogen Binding

ABSTRACTThe fibronectin-binding protein A (FnBPA) is a cell surface-associated protein ofStaphylococcus aureuswhich mediates adherence to the host extracellular matrix and is important for bacterial virulence. Previously, substantial sequence diversity was found among strains in the fibrinogen-binding A domain of this protein, and 7 different isotypes were described. The effect of this sequence diversity on the human antibody response, in terms of both antibody production and antibody function, remains unclear. In this study, we identify five different FnBPA A domain isotypes based on the sequence results of 22 clinicalS. aureusisolates, obtained from the same number of patients suffering from bacteremia. Using a bead-based Luminex technique, we measure the patients’ total immunoglobulin G (IgG) against the 7 FnBPA isotypes at the onset and during the time course of bacteremia (median of 10 serum samples per patient over a median of 35 days). A significant increase in IgG against the FnBPA A domain, including the isotype carried by the infecting strain, is observed in only three out of 22 patients (14%) after the onset of bacteremia. Using a Luminex-based FnBPA–fibrinogen-binding assay, we find that preincubation of recombinant FnBPA isotypes with IgG from diverse patients does not interfere with binding to fibrinogen. This observation is confirmed using an alternative Luminex-based assay and enzyme-linked immunosorbent assay (ELISA).IMPORTANCEDespite the manyin vitroand murinein vivostudies involving FnBPA, the actual presence of this virulence factor during human infection is less well established. Furthermore, it is currently unknown to what extent sequence variation in such a virulence factor affects the human antibody response and the ability of antibodies to interfere with FnBPA function. This study sheds new light on these issues. First, the uniform presence of a patient’s IgG against FnBPA indicates the presence and importance of this virulence factor duringS. aureuspathogenesis. Second, the absence of an increase in antibody production in most patients following bacteremia indicates the complexity ofS. aureus-host interactions, possibly involving immune evasion or lack of expression of FnBPA during invasive infection. Finally, we provide new insights into the inability of human antibodies to interfere with FnBPA-fibrinogen binding. These observations should be taken into account during the development of novel vaccination approaches.

scholarly journals Secretion of a bacterial virulence factor is driven by the folding of a C-terminal segment

2010 ◽  
Vol 107 (41) ◽  
pp. 17739-17744 ◽  
Author(s):  
Janine H. Peterson ◽  
Pu Tian ◽  
Raffaele Ieva ◽  
Nathalie Dautin ◽  
Harris D. Bernstein
Keyword(s):  
Virulence Factor ◽  
Terminal Segment ◽  
Bacterial Virulence ◽  
Bacterial Virulence Factor

Dual function of coronatine as a bacterial virulence factor against plants: possible COI1–JAZ-independent role

RSC Advances ◽  
2016 ◽  
Vol 6 (23) ◽  
pp. 19404-19412 ◽  
Author(s):  
Syusuke Egoshi ◽  
Yousuke Takaoka ◽  
Hiroaki Saito ◽  
Yuuki Nukadzuka ◽  
Kengo Hayashi ◽  
...  
Keyword(s):  
Virulence Factor ◽  
Mode Of Action ◽  
Bacterial Virulence ◽  
Dual Function ◽  
Dual Mode ◽  
Bacterial Virulence Factor

A phytotoxin coronatine has a dual mode of action, triggering stomatal reopening through COI1–JAZ-dependent and independent pathways.

scholarly journals Active-Site Flexibility and Substrate Specificity in a Bacterial Virulence Factor: Crystallographic Snapshots of an Epoxide Hydrolase

Structure ◽  
2017 ◽  
Vol 25 (5) ◽  
pp. 697-707.e4 ◽  
Author(s):  
Kelli L. Hvorecny ◽  
Christopher D. Bahl ◽  
Seiya Kitamura ◽  
Kin Sing Stephen Lee ◽  
Bruce D. Hammock ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Virulence Factor ◽  
Active Site ◽  
Epoxide Hydrolase ◽  
Bacterial Virulence ◽  
Bacterial Virulence Factor

scholarly journals Chicoric acid binds to two sites and decreases the activity of the YopH bacterial virulence factor

Oncotarget ◽  
2016 ◽  
Vol 7 (3) ◽  
pp. 2229-2238 ◽  
Author(s):  
Alicja Kuban-Jankowska ◽  
Kamlesh K. Sahu ◽  
Magdalena Gorska ◽  
Jack A. Tuszynski ◽  
Michal Wozniak
Keyword(s):  
Virulence Factor ◽  
Bacterial Virulence ◽  
Chicoric Acid ◽  
Bacterial Virulence Factor

scholarly journals M Protein, a Classical Bacterial Virulence Determinant, Forms Complexes with Fibrinogen that Induce Vascular Leakage

Cell ◽  
2004 ◽  
Vol 116 (3) ◽  
pp. 367-379 ◽  
Author(s):  
Heiko Herwald ◽  
Henning Cramer ◽  
Matthias Mörgelin ◽  
Wayne Russell ◽  
Ulla Sollenberg ◽  
...  
Keyword(s):  
Protein A ◽  
Bacterial Virulence ◽  
Vascular Leakage ◽  
M Protein ◽  
Virulence Determinant
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