Immunoglobulin-binding domains of peptostreptococcal protein L enhance vaginal colonization of mice by Streptococcus gordonii

2001 ◽  
Vol 30 (4) ◽  
pp. 229-235 ◽  
Author(s):  
Susanna Ricci ◽  
Donata Medaglini ◽  
Harold Marcotte ◽  
Arne Olsén ◽  
Gianni Pozzi ◽  
...  
Keyword(s):  
Streptococcus Gordonii ◽  
Protein L ◽  
Binding Domains ◽  
Vaginal Colonization ◽  
Immunoglobulin Binding

scholarly journals Immunoglobulin-binding domains: Protein L from Peptostreptococcus magnus

2003 ◽  
Vol 31 (3) ◽  
pp. 716-718 ◽  
Author(s):  
N.G. Housden ◽  
S. Harrison ◽  
S.E. Roberts ◽  
J.A. Beckingham ◽  
M. Graille ◽  
...  
Keyword(s):  
Binding Sites ◽  
Protein A ◽  
Cell Wall Protein ◽  
Protein G ◽  
Protein L ◽  
Heavy Chains ◽  
Binding Domains ◽  
Peptostreptococcus Magnus ◽  
Immunoglobulin Binding

Protein L is a multidomain cell-wall protein isolated from Peptostreptococcus magnus. It belongs to a group of proteins that contain repeated domains that are able to bind to Igs without stimulating an immune response, the most characterized of this group being Protein A (Staphylococcus aureus) and Protein G (Streptococcus). Both of these proteins bind predominantly to the interface of CH2-CH3 heavy chains, while Protein L binds exclusively to the VL domain of the κ-chain. The function of these proteins in vivo is not clear but it is thought that they enable the bacteria to evade the host's immune system. Two binding sites for κ-chain on a single Ig-binding domain from Protein L have recently been reported and we give evidence that one site has a 25–55-fold higher affinity for κ-chain than the second site.

scholarly journals Plasma Half-life Extension of Small Recombinant Antibodies by Fusion to Immunoglobulin-binding Domains

2011 ◽  
Vol 287 (7) ◽  
pp. 4462-4469 ◽  
Author(s):  
Meike Hutt ◽  
Aline Färber-Schwarz ◽  
Felix Unverdorben ◽  
Fabian Richter ◽  
Roland E. Kontermann
Keyword(s):  
Half Life ◽  
Recombinant Antibodies ◽  
Life Extension ◽  
Binding Domains ◽  
Immunoglobulin Binding ◽  
Plasma Half Life

Studies on a single immunoglobulin-binding domain of protein L from Peptostreptococcus magnus: the role of tyrosine-53 in the reaction with human IgG

2001 ◽  
Vol 353 (2) ◽  
pp. 395-401 ◽  
Author(s):  
Jennifer A. BECKINGHAM ◽  
Nicholas G. HOUSDEN ◽  
Nicola M. MUIR ◽  
Stephen P. BOTTOMLEY ◽  
Michael G. GORE
Keyword(s):  
Chain Complex ◽  
Binding Domain ◽  
Protein L ◽  
Human Igg ◽  
Tyrosine Residues ◽  
Kd Values ◽  
Trp Mutant ◽  
The Stability ◽  
Immunoglobulin Binding

Chemical modification experiments with tetranitromethane (TNM) have been used to investigate the role of tyrosine residues in the formation of the complex between PpL (the single Ig-binding domain of protein L, isolated from P. magnus strain 3316) and the kappa light chain (κ-chain). Reaction of PpL with TNM causes the modification of 1.9 equiv. of tyrosine (Tyr51 and Tyr53) and results in an approx. 140-fold decrease in affinity for human IgG. Similar experiments with mutated PpL proteins suggest that nitration predominantly inactivates the protein by modification of Tyr53. Reduction of the nitrotyrosine groups to aminotyrosine by incubation with sodium hydrosulphite does not restore high affinity for IgG. Modification of κ-chain by TNM resulted in the nitration of 3.1±0.09 tyrosine residues. When the PpLŐκ-chain complex was incubated with TNM, 4.1±0.04 tyrosine residues were nitrated, indicating that one tyrosine residue previously modified by the reagent was protected from TNM when the proteins are in complex with each other. The Kd for the equilibrium between PpL, human IgG and their complex has been shown by ELISA to be 112±20nM. A similar value (153±33nM) was obtained for the complex formed between IgG and the Tyr64 → Trp mutant (Y64W). However, the Kd values for the equilibria involving the PpL mutants Y53F and Y53F,Y64W were found to be 3.2±0.2 and 4.6±1µM respectively. These suggest that the phenol group of Tyr53 in PpL is important to the stability of the PpLŐκ-chain complex.

scholarly journals Detecting total immunoglobulins in diverse animal species with a novel split enzymatic assay

2019 ◽  
Vol 15 (1) ◽  
Author(s):  
Marija Drikic ◽  
Steven Olsen ◽  
Jeroen De Buck
Keyword(s):  
G Protein ◽  
Binding Proteins ◽  
Animal Species ◽  
Protein A ◽  
Enzyme Linked Immunosorbent Assay ◽  
Protein G ◽  
Protein L ◽  
Strong Signal ◽  
Number Of Species ◽  
Immunoglobulin Binding

Abstract Background Total immunolobulin G concentration is a useful, albeit underutilized, diagnostic parameter for health assessments of non-domestic animal species, due to a lack of functional diagnostic tools. Traditional assays, including enzyme-linked immunosorbent assay or radial immunodiffusion, require development of specific reagents (e.g., polyclonal antisera and appropriate protocols) for each animal species, precluding wide and easy adoption in wildlife welfare. As an alternative, bacterial virulence factors able to bind IgGs in antigen-independent manner can be used. To further simplify the diagnostic procedure and increase the number of species recognized by an assay, in this study a recently developed Split Trehalase immunoglobulin assay (STIGA) with bIBPs as a sensing elements was used to detect antibodies in 29 species from 9 orders. Three bacterial immunoglobulin binding proteins (protein G, protein A and protein L) were incorporated into STIGA reagents to increase the number of species recognized. Results IgG concentrations were detected through glucose production and produced signals were categorized in 4 categories, from not active to strong signal. Activation was detected in almost all tested animal species, apart from birds. Incorporation of Protein G, Protein A and Protein L allowed detection of IgGs in 62, 15.5 and 6.9% of species with a strong signal, respectively. Assays combining 2 bacterial immunoglobulin binding proteins as sensing element generally gave poorer performance than assays with the same bacterial immunoglobulin binding proteins fused to both trehalase fragments. Conclusions STIGA assays have potential to be further developed into an easily adoptable diagnostic test for total amount of IgGs in almost any serum sample, independent of species.

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