Isolation and properties of a novel IgG-binding protein from streptococci of serological group U

1987 ◽  
Vol 176 (1) ◽  
Author(s):  
GursharanS. Chhatwal ◽  
Hans Blobel
Keyword(s):  
Binding Protein ◽  
Serological Group ◽  
Igg Binding

scholarly journals Prolonged display or rapid internalization of the IgG-binding protein ZZ anchored to the surface of cells using the diphtheria toxin T domain

2001 ◽  
Vol 14 (6) ◽  
pp. 439-446 ◽  
Author(s):  
Philippe Nizard ◽  
Alexandre Chenal ◽  
Bruno Beaumelle ◽  
Alain Fourcade ◽  
Daniel Gillet
Keyword(s):  
Diphtheria Toxin ◽  
Binding Protein ◽  
Igg Binding ◽  
T Domain

Characterization of a gene coding for a type IIo bacterial IgG-binding protein

1995 ◽  
Vol 32 (9) ◽  
pp. 669-678 ◽  
Author(s):  
Michael D.P. Boyle ◽  
Josephine Weber-Heynemann ◽  
Roberta Raeder ◽  
Andreas Podbielski
Keyword(s):  
Binding Protein ◽  
Gene Coding ◽  
Igg Binding

Synthesis and mutagenesis of an IgG-binding protein based upon protein A of Staphylococcus aureus

1991 ◽  
Vol 4 (8) ◽  
pp. 963-970 ◽  
Author(s):  
Andrew G. Popplewell ◽  
Micheal G. Gore ◽  
Michael Scawen ◽  
Tony Atkinson
Keyword(s):  
Staphylococcus Aureus ◽  
Binding Protein ◽  
Protein A ◽  
Igg Binding

pH-sensitive interactions between IgG and a mutated IgG-binding protein based upon two B domains of Protein A from Staphylococcus aureus

1992 ◽  
Vol 5 (6) ◽  
pp. 577-582 ◽  
Author(s):  
Michael G. Gore ◽  
William F. Ferris ◽  
Andrew G. Popplewell ◽  
Michael Scawen ◽  
Tony Atkinson
Keyword(s):  
Staphylococcus Aureus ◽  
Binding Protein ◽  
Protein A ◽  
Ph Sensitive ◽  
Igg Binding

Site-directed lipid modification of IgG-binding protein by intracellular bacterial lipoprotein process

1999 ◽  
Vol 75 (1) ◽  
pp. 23-31 ◽  
Author(s):  
Hideki Shigematsu ◽  
Takashi Ebihara ◽  
Yasuko Yanagida ◽  
Tetsuya Haruyama ◽  
Eiry Kobatake ◽  
...  
Keyword(s):  
Binding Protein ◽  
Lipid Modification ◽  
Igg Binding ◽  
Bacterial Lipoprotein

scholarly journals Recombinant Streptococcus equi Proteins Protect Mice in Challenge Experiments and Induce Immune Response in Horses

2004 ◽  
Vol 72 (6) ◽  
pp. 3228-3236 ◽  
Author(s):  
Margareta Flock ◽  
Karin Jacobsson ◽  
Lars Frykberg ◽  
Timothy R. Hirst ◽  
Anders Franklin ◽  
...  
Keyword(s):  
Protective Efficacy ◽  
Binding Protein ◽  
Serum Antibody ◽  
Control Group ◽  
Nasal Colonization ◽  
Igg Antibody ◽  
Igg Binding ◽  
Streptococcus Equi ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding

ABSTRACT Horses that have undergone infection caused by Streptococcus equi subspecies equi (strangles) were found to have significantly increased serum antibody titers against three previously characterized proteins, FNZ (cell surface-bound fibronectin binding protein), SFS (secreted fibronectin binding protein), and EAG (α2-macroglobulin, albumin, and immunoglobulin G [IgG] binding protein) from S. equi. To assess the protective efficacy of vaccination with these three proteins, a mouse model of equine strangles was utilized. Parts of the three recombinant proteins were used to immunize mice, either subcutaneously or intranasally, prior to nasal challenge with S. equi subsp. equi. The adjuvant used was EtxB, a recombinant form of the B subunit of Escherichia coli heat-labile enterotoxin. It was shown that nasal colonization of S. equi subsp. equi and weight loss due to infection were significantly reduced after vaccination compared with a mock-vaccinated control group. This effect was more pronounced after intranasal vaccination than after subcutaneous vaccination; nearly complete eradication of nasal colonization was obtained after intranasal vaccination (P < 0.001). When the same antigens were administered both intranasally and subcutaneously to healthy horses, significant mucosal IgA and serum IgG antibody responses against FNZ and EAG were obtained. The antibody response was enhanced when EtxB was used as an adjuvant. No adverse effects of the antigens or EtxB were observed. Thus, FNZ and EAG in conjunction with EtxB are promising candidates for an efficacious and safe vaccine against strangles.

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