scholarly journals Identification of novel pig and human immunoglobulin G-binding proteins and characterization of the binding regions of enolase from Streptococcus suis serotype 2

2020 ◽  
Author(s):  
Quan Li ◽  
Yang Fu ◽  
Genglin Guo ◽  
Zhuohao Wang ◽  
Wei Zhang
Keyword(s):  
Western Blot ◽  
Immunoglobulin G ◽  
Binding Proteins ◽  
Streptococcus Suis ◽  
Factor H ◽  
Surface Proteins ◽  
Host Immune System ◽  
Dot Blot ◽  
Binding Regions ◽  
Far Western Blot

Abstract Streptococcus suis, a major emerging pathogen in swine and humans, expresses immunoglobulin G (IgG)-binding proteins (IBPs), which contribute to the ability of organism to evasion of host immune system. The objective of this study was to identify novel pig IgG (pIgG) and human IgG (hIgG)-binding proteins and characterize the binding regions of enolase from Streptococcus suis serotype 2 (S. suis 2). Here, four pIgG-binding proteins (pIBPs) and five hIgG-binding proteins (hIBPs) were identified from S. suis 2 surface proteins by 2D-Far-western blot assays. All the newly captured proteins were expressed and further confirmed their binding activity to pIgG or hIgG by Far-western blot and dot blot. In addition to previously identified factor H, fibronectin, collagen, fibrinogen, plasminogen and laminin, we also found that both pIgG and hIgG can specifically interact with enolase. Binding assays indicated that interactions of S. suis 2 enolase with pIgG and hIgG is primarily mediated by the enolase C-terminal portion (Enolase-C, a.a. 142-432). We found that hIgG exhibited stronger binding ability to Enolase-C than pIgG. Further analysis of the C-terminal regions of enolase (Enolase-C1 and Enolase-C2) suggested that the C-terminus possessed two different binding domains with distinct host IgG proteins. Strikingly, we confirmed that pIgG interacted with the Enolase-C1 (a.a. 142-271) and hIgG interacted with the Enolase-C2 (a.a. 271-432). These observations of enolase provide interesting insights in the pathogenesis of S. suis infection.

scholarly journals Identification of novel pig and human immunoglobulin G-binding proteins and characterization of the binding regions of enolase from Streptococcus suis serotype 2

2020 ◽  
Author(s):  
Quan Li ◽  
Yang Fu ◽  
Genglin Guo ◽  
Zhuohao Wang ◽  
Wei Zhang
Keyword(s):  
Western Blot ◽  
Immunoglobulin G ◽  
Binding Proteins ◽  
Streptococcus Suis ◽  
Factor H ◽  
Surface Proteins ◽  
Host Immune System ◽  
Dot Blot ◽  
Binding Regions ◽  
Far Western Blot

Abstract Streptococcus suis, a major emerging pathogen in swine and humans, expresses immunoglobulin G (IgG)-binding proteins (IBPs), which contribute to the ability of organism to evasion of host immune system. The objective of this study was to identify novel pig IgG (pIgG) and human IgG (hIgG)-binding proteins and characterize the binding regions of enolase from Streptococcus suis serotype 2 (S. suis 2). Here, four pIgG-binding proteins (pIBPs) and five hIgG-binding proteins (hIBPs) were identified from S. suis 2 surface proteins by 2D-Far-western blot assays. All the newly captured proteins were expressed and further confirmed their binding activity to pIgG or hIgG by Far-western blot and dot blot. In addition to previously identified factor H, fibronectin, collagen, fibrinogen, plasminogen and laminin, we also found that both pIgG and hIgG can specifically interact with enolase. Binding assays indicated that interactions of S. suis 2 enolase with pIgG and hIgG is primarily mediated by the enolase C-terminal portion (Enolase-C, a.a. 142-432). We found that hIgG exhibited stronger binding ability to Enolase-C than pIgG. Further analysis of the C-terminal regions of enolase (Enolase-C1 and Enolase-C2) suggested that the C-terminus possessed two different binding domains with distinct host IgG proteins. Strikingly, we confirmed that pIgG interacted with the Enolase-C1 (a.a. 142-271) and hIgG interacted with the Enolase-C2 (a.a. 271-432). These observations of enolase provide interesting insights in the pathogenesis of S. suis infection.

scholarly journals Immunoblotting Detection of Immunoglobulin G Post Subcutaneous Immunization Of Protein Hemaglutinin Pili Klebsiella pneumoniae 12,8 kDa on Mice BALB / C

2017 ◽  
Vol 3 (2) ◽  
pp. 40 ◽  
Author(s):  
Dini Agustina
Keyword(s):  
Klebsiella Pneumoniae ◽  
Western Blot ◽  
Immunoglobulin G ◽  
Quantitative Result ◽  
Protein Subunit ◽  
Dot Blot ◽  
Humoral Immune ◽  
Hemagglutinin Protein ◽  
Encapsulated Bacteria ◽  
Subcutaneous Immunization

Klebsiella pneumoniae is the second most common cause of community infection and nosocomial infections due to Gram-negative bacteria. These bacteria are able to induce the onset of immune response, especially humoral immune response.Humoral immunity acts through the activation of B cells that produce antibodies. Antibodies, especially IgG, will cause encapsulated bacteria such as Klebsiella pneumoniae to be better phagocytosed. The purpose of this study was to determine the IgG response to hemagglutinin protein pili K. pneumoniae 12.8 kDa. The method used in this research is Immunoblotting method with western blot and dot blot. The primary antibodies used for the western blot and dot blot tests were isolated from BALB / C mice serum induced with the subcutaneous pili K. pneumoniae 12.8 kDa protein. To get the standard in assessing the results of dot blot were used Corel Photo-paint X6. The semi-quantitative result of dot blot was obtained with the strongest reaction of the antibody dilution at 1/100 while the antigen dilution titer at 1 / 10.000. Results from western blotting showed a positive reaction of the pili protein subunit with a molecular weight of 128.1 kDa, 114.4 kDa, 64.9 kDa, 31.1 kDa, 27.7 kDa, 24.8 kDa, 20.9 kDa, 12.8 kDa, and 10 kDa. The conclusion of this study is the immunization of hemagglutinin pili K. pneumoniae 12.8 kDa subcutaneously capable of inducing the formationof Immunoglobulin G in BALB / C mice.

scholarly journals Factor H specifically capture novel Factor H-binding proteins of Streptococcus suis and contribute to the virulence of the bacteria

2017 ◽  
Vol 196 ◽  
pp. 17-25 ◽  
Author(s):  
Quan Li ◽  
Caifeng Ma ◽  
Yang Fu ◽  
Yanan He ◽  
Yanfei Yu ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Streptococcus Suis ◽  
Factor H

scholarly journals Temporal Analysis of Borrelia burgdorferiErp Protein Expression throughout the Mammal-Tick InfectiousCycle

2003 ◽  
Vol 71 (12) ◽  
pp. 6943-6952 ◽  
Author(s):  
Jennifer C. Miller ◽  
Kate von Lackum ◽  
Kelly Babb ◽  
Jason D. McAlister ◽  
Brian Stevenson
Keyword(s):  
Temporal Analysis ◽  
Factor H ◽  
Innate Immune ◽  
Surface Proteins ◽  
Host Immune System ◽  
Innate Immune Responses ◽  
Outer Surface Proteins ◽  
Mammalian Infection ◽  
Infectious Cycle

ABSTRACT Previous immunological studies indicated that the Lyme disease spirochete, Borrelia burgdorferi, expresses Erp outer surface proteins during mammalian infection. We conducted analyses of Erp expression throughout the entire tick-mammal infectious cycle, which revealed that the bacteria regulate Erp production in vivo. Bacteria within unfed nymphal ticks expressed little to no Erp proteins. However, as infected ticks fed on mice, B. burgdorferi increased production of Erp proteins, with essentially all transmitted bacteria expressing these proteins. Mice infected with B. burgdorferi mounted rapid IgM responses to all tested Erp proteins, followed by strong immunoglobulin G responses that generally increased in intensity throughout 11 months of infection, suggesting continued exposure of Erp proteins to the host immune system throughout chronic infection. As naive tick larvae acquired B. burgdorferi by feeding on infected mice, essentially all transmitted bacteria produced Erp proteins, also suggestive of continual Erp expression during mammalian infection. Shortly after the larvae acquired bacteria, Erp production was drastically downregulated. The expression of Erp proteins on B. burgdorferi throughout mammalian infection is consistent with their hypothesized function as factor H-binding proteins that protect the bacteria from host innate immune responses.

scholarly journals Detection of immunoglobulin-G-binding proteins in Streptococcus suis

1993 ◽  
Vol 139 (12) ◽  
pp. 2953-2958 ◽  
Author(s):  
B. Serhir ◽  
R. Higgins ◽  
B. Foiry ◽  
M. Jacques
Keyword(s):  
Immunoglobulin G ◽  
Binding Proteins ◽  
Streptococcus Suis

scholarly journals Fhb, a Novel Factor H-Binding Surface Protein, Contributes to the Antiphagocytic Ability and Virulence of Streptococcus suis

2012 ◽  
Vol 80 (7) ◽  
pp. 2402-2413 ◽  
Author(s):  
Yaya Pian ◽  
Shuzhen Gan ◽  
Shujie Wang ◽  
Jie Guo ◽  
Pingping Wang ◽  
...  
Keyword(s):  
Binding Protein ◽  
Surface Protein ◽  
Streptococcus Suis ◽  
Invasive Disease ◽  
Binding Activity ◽  
Repeat Sequence ◽  
Factor H ◽  
Surface Proteins ◽  
Infection Model ◽  
Content Type

ABSTRACTStreptococcus suisserotype 2 is a Gram-positive bacterium that causes sepsis and meningitis in piglets and humans. The mechanisms ofS. suisserotype 2 invasive disease are not well understood. The surface proteins of pathogens usually play important roles in infection and bacterium-host interactions. Here, we identified a novel surface protein that contributed significantly to the virulence ofS. suisserotype 2 in a piglet infection model. This protein showed little similarity to other reported proteins and exhibited strong binding activity to human factor H (hFH). It was designated Fhb (factor H-binding protein). Thefhbgenes found inS. suisserotypes 1, 2, 4, 7, and 9 exhibited molecular polymorphism. Fhb possessed two proline-rich repeat sequences and XPZ domains, and one repeat sequence exhibited a high homology to Bac, an IgA-binding protein ofStreptococcus agalactiae. Evidence strongly indicated thatfhb-deficient mutants had diminished phagocytosis resistance in bactericidal assays. In addition, Fhb plays important roles in complement-mediated immunity by interacting with hFH. These findings indicated that Fhb is a crucial surface protein contributing to the virulence ofS. suis, with important functions in evading innate immune defenses by interaction with host complement regulatory factor hFH.

Sign in / Sign up

Export Citation Format

Share Document