scholarly journals PURIFIED IGG F C-BINDING PROTEINS FROM M22 GROUP A STREPTOCOCCUS ARE ABLE TO INDUCE EXPERIMENTAL GLOMERULONEPHRITIS

2014 ◽  
Vol 14 (4-5) ◽  
pp. 383
Author(s):  
L. A. Burova ◽  
P. V. Pigarevsky ◽  
E. A. Gavrilova ◽  
V. G. Seliverstova ◽  
K. Schalen ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Group A Streptococcus ◽  
Experimental Glomerulonephritis ◽  
Group A

Role of group A streptococcal IgG-binding proteins in triggering experimental glomerulonephritis in the rabbit

Apmis ◽  
2003 ◽  
Vol 111 (10) ◽  
pp. 955-962 ◽  
Author(s):  
LARISSA BUROVA ◽  
ANETTE THERN ◽  
PITER PIGAREVSKY ◽  
MARIA GLADILINA ◽  
VALENTINA SELIVERSTOVA ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Experimental Glomerulonephritis ◽  
Igg Binding ◽  
Group A

scholarly journals Identification and Characterization of a Novel Secreted Immunoglobulin Binding Protein from Group A Streptococcus

2001 ◽  
Vol 69 (8) ◽  
pp. 4851-4857 ◽  
Author(s):  
Peter K. Fagan ◽  
Dieter Reinscheid ◽  
Birgit Gottschalk ◽  
Gursharan S. Chhatwal
Keyword(s):  
Binding Proteins ◽  
Group A Streptococcus ◽  
Binding Protein ◽  
Coiled Coil ◽  
Invasive Disease ◽  
Local Similarity ◽  
M Proteins ◽  
Immunoglobulin Binding Protein ◽  
Group A ◽  
Immunoglobulin Binding

ABSTRACT Immunoglobulin binding proteins are one of several pathogenicity factors which have been associated with invasive disease caused by group A streptococci. The surface-bound M and M-like proteins ofStreptococcus pyogenes are the most characterized of these immunoglobulin binding proteins, and in most cases they bind only a single antibody class. Here we report the identification of a novel non-M-type secreted protein, designated SibA (for secreted immunoglobulin binding protein from group A streptococcus), which binds all immunoglobulin G (IgG) subclasses, the Fc and Fab fragments, and also IgA and IgM. SibA has no significant sequence homology to any M-related proteins, is not found in the vir regulon, and contains none of the characteristic M-protein regions, such as the A or C repeats. Like M proteins, however, SibA does have relatively high levels of alanine, lysine, glutamic acid, leucine, and glycine. SibA and M proteins also share an alpha-helical N-terminal secondary structure which has been previously implicated in immunoglobulin binding in M proteins. Evidence presented here indicates that this is also the case for SibA. SibA also has regions of local similarity with other coiled-coil proteins such as Listeria monocytogenes P45 autolysin, human myosin heavy chain, macrogolgin, and Schistoma mansoni paramyosin, some of which are of potential significance since cross-reactive antibodies between myosin proteins and M proteins have been implicated in the development of the autoimmune sequelae of streptococcal disease.

Protein M and Fibronectin-Binding Proteins are Not Sufficient to Promote Internalization of Group a Streptococci into Hela Cells

1998 ◽  
Vol 11 (3) ◽  
pp. 163-169 ◽  
Author(s):  
R. Greco ◽  
C. von Hunolstein ◽  
G. Orefici ◽  
G. Donnarumma ◽  
M. Polidoro ◽  
...  
Keyword(s):  
Hela Cells ◽  
Binding Proteins ◽  
Group A Streptococcus ◽  
Protein A ◽  
Group A Streptococci ◽  
Cell Monolayers ◽  
Invasive Diseases ◽  
Internalization Process ◽  
Group A ◽  
Fibronectin Binding

Infection by group A streptococci is often associated with highly invasive diseases resulting in sepsis and shock. Recently, this species has renewed interest in the mechanism by which some strains are better able to invade mucosal epithelia and to penetrate into the bloodstream than are others. In this work we have evaluated the invasive ability of eight group A Streptococcus pyogenes strains isolated either from patients with severe invasive diseases, or with pharyngitis, or from healthy carrier. Five out of the eight strains studied were efficiently internalized within HeLa cells and, of these, four produced the M6 protein. A recombinant S.gordonii strain constitutively expressing the M6 protein failed to invade HeLa cell monolayers, suggesting that the expression of the M6 protein is not sufficient to allow the non-invasive S.gordonii to be internalized within Hela cells. As fibronectin-binding proteins have been implicated as primary adhesins in host-parasite interactions, we assayed the adhesiveness and the invasiveness of five invasive GAS strains in competition experiments where HeLa cells were infected with bacteria in the presence of purified fibronectin. The results obtained indicated that fibronectin moderately inhibits bacterial adhesion, while it does not affect internalization. These results indicate that other factors, together with fibronectin-binding proteins, participate in the adhesion of streptococci, and that fibronectin-mediated adhesion does not seem to be important in the internalization process of streptococci within HeLa cells.

scholarly journals Impact of IgG Fc-fragments on experimental glomerulonephritis induced by Streptococcus pyogenes strain binding various immunoglobulin classes

2020 ◽  
Vol 10 (1) ◽  
pp. 55-63
Author(s):  
L. A. Burova ◽  
P. V. Pigarevsky ◽  
V. A. Snegova ◽  
A. A. Totolian
Keyword(s):  
Immune Complexes ◽  
Binding Proteins ◽  
Rabbit Model ◽  
Renal Tissue ◽  
Proliferative Glomerulonephritis ◽  
Pathological Changes ◽  
Experimental Glomerulonephritis ◽  
Rabbit Igg ◽  
Group A

The pathogenesis of poststreptococcal glomerulonephritis (PSGN), a major complication of acute infections caused by group A streptococci (GAS) remains unclear. Several theories, based on the role of certain streptococcal virulence factors, as well as immunological mimicry between GAS and renal tissue, have been proposed. Earlier, we reported that many virulent clinical GAS isolates showing confirmed nephritogenic activity were capable of nonimmune Fc binding of monomeric or aggregated IgG. Moreover, a rabbit model of PSGN allowed to obtain findings regarding a crucial role of streptococcal IgG Fc binding proteins belonging to the M family surface proteins, in the onset of PSGN. Rabbits injected with inactivated IgGFcBP-positive streptococci, acquired changes in the renal tissue with deposited IgG and complement C3, as well as signs of immune inflammation characteristic for human PSGN. Also, it was shown that the induction of experimental glomerulonephritis could be inhibited after normal IgG or its purified Fc fragments were inoculated at early stages of the process. The data obtained in rabbits injected with group A streptococcal type M60 also showed pathogenic functions of the IgA Fc-binding proteins of GAS. The aim of the study was to examine inhibiting activity of the purified rabbit IgG Fc fragments on the manifestations of glomerulonephritis induced by S. pyogenes strains capable of binding diverse forms of immunoglobulins such native IgG, immune complexes, and IgA.Materials and methods. GAS strains of emml, emml2 and emm60 genotypes were used to induce PSGN or IgA-nephropa-thy in rabbits. Fc fragments derived from rabbit IgG were obtained by enzymatic digestion and purified by affinity chromatography on a protein G-sepharose FF column. Immunomorphological changes of renal tissue were estimated by morphometric analysis.Results. In the present study, using the rabbit model, we revealed pathological changes of different intensity and localization in the renal tissue. For streptococci of the emm1 and emm12 genotypes, PSGN was characterized by deposition of IgG or IgG-anti-IgG immune complexes within the basal glomerular membrane. Morphological changes were evaluated as a membranous-proliferative glomerulonephritis. Meanwhile, IgA-glomerulonephritis is characterized by deposition of IgA in mesangial cells of glomeruli, leading to the mesangial-proliferative glomerulonephritis or IgA-nephropathy. Intravenously administered purified Fc fragments derived from normal rabbit IgG varied in effects on pathological processes: (i) IgG Fc fragments of fully inhibited development of the PSGN induced by IgG Fc binding strain of emml genotype, (ii) IgG Fc fragments of partially reverted changes caused by the emm12 genotype strain, which was binding only to immune complexes, and (iii) had no effects on pathological changes caused by the emm60 genotype GAS strain, which was binding only IgA.Conclusion. The data obtained point and emergence of differences in mechanisms of renal lesions development at glomerulonephritis, depending on the emm genotype of GAS strain. In addition, it also confirmed GAS-derived involvement for various IgFc-receptor proteins in the pathology. Further studies on potential prophylactic or curative effects of IgG Fc fragments in PSGN should therefore be of interest. The findings might suggest a new therapeutic approach for non-suppurative poststreptococcal diseases.

Etiology, clinical presentation, laboratory diagnostics, pathogenesis of impetigo and treatment methods

2020 ◽  
pp. 64-70
Author(s):  
Anastasiya Laknitskaya
Keyword(s):  
Streptococcus Pyogenes ◽  
Skin Diseases ◽  
Group A Streptococcus ◽  
Antibiotic Sensitivity ◽  
Antioxidant Defense System ◽  
Laboratory Diagnostics ◽  
Treatment Methods ◽  
Group A ◽  
The Individual

Currently, one of the priority medical and social problems is the optimization of treatment methods for pyoderma associated with Streptococcus pyogenes — group A streptococcus (GAS). To date, the proportion of pyoderma, the etiological factor of which is Streptococcus pyogenes, is about 6 % of all skin diseases and is in the range from 17.9 to 43.9 % of all dermatoses. Role of the bacterial factor in the development of streptococcal pyoderma is obvious. Traditional treatment complex includes antibacterial drugs selected individually, taking into account the antibiotic sensitivity of pathognomonic bacteria, and it is not always effective. Currently implemented immunocorrection methods often do not take into account specific immunological features of the disease, the individual, and the fact that the skin performs the function of not only a mechanical barrier, but it is also an immunocompetent organ. Such an approach makes it necessary to conduct additional studies clarifying the role of factors of innate and adaptive immunity, intercellular mediators and antioxidant defense system, that allow to optimize the treatment of this pathology.

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