Antibody orientation at bacterial surfaces is related to invasive infection

Nordenfelt, Pontus; Waldemarson, Sofia; Linder, Adam; Mörgelin, Matthias; Karlsson, Christofer; Malmström, Johan; Björck, Lars

doi:10.1084/jem.20120325

Cited by 99 publications

(133 citation statements)

References 51 publications

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“…Pre-adsorption of PG to Pt sensor surfaces enhances the specific binding of the Fc region of mammalian IgG [3]. This oriented attachment of antibody [5] [7] serves to expose the Fab region, which maximizes the tethering capability for immunoprecipitation of antigens.…”

Section: Resultsmentioning

confidence: 99%

“…The physiologic function of this Fc:PG binding serves to facilitate bacterial infection and avoidance of the host's immune system by nonspecifically coating bacteria with host antibodies [6]. Antibodies bound to PG are oriented with the antigen specific binding pockets facing outwards, away from the pathogen [5] [7]. This ability to specifically bind antibodies aligned in a precise orientation has been utilized to develop antibody-based detection systems [8]- [10].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Streptococcal Protein G Enhances Antibody Binding to Platinum Sensor Surfaces

Stephens¹,

Ellis²,

Huebner³

et al. 2015

JST

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Photo-Electric Microbe Sensor is a patented biotechnology that detects microbes in aqueous solution by measuring the change in photo-voltage in response to UV light stimulation of a platinum (Pt) disk surface on an electrode before and after immunoprecipitation of microbes. This study aimed to increase the sensitivity of microbe detection by pre-adsorbing recombinant Streptococcal Protein G (PG), to the Pt sensor surface. Streptococcal PG binds the Fc region of mammalian IgG molecules and we investigated the association of PG to Pt and the resulting ability to tether antibodies to the Pt-PG surface. An ELISA protocol was optimized to detect the presence of mouse monoclonal antibodies tethered to Pt immunoaffinity disks, and to determine the recommended blocking solution and reagent concentrations. Our results demonstrate that PG binds to bare Pt, increases IgG affinity to the Pt surface following Superblock Buffer application, and together offers design-options for Pt-based sensor technologies.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Streptococcal Protein G Enhances Antibody Binding to Platinum Sensor Surfaces

Stephens¹,

Ellis²,

Huebner³

et al. 2015

JST

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“…This phenomenon contrasts with labeling of bacteria with IgG antibodies upon cleavage by IdeS. Björk et al showed that IgG Fab fragments remain attached to the bacterial surface upon IgG cleavage [28]. We propose that the detachment of IgM F(ab’)2 fragments is due to the lower affinity of IgM binding [29].…”

Section: Discussionmentioning

confidence: 96%

IgM cleavage by Streptococcus suis reduces IgM bound to the bacterial surface and is a novel complement evasion mechanism

et al. 2018

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Streptococcus suis (S. suis) causes meningitis, arthritis and endocarditis in piglets. The aim of this study was to characterize the IgM degrading enzyme of S. suis (IdeSsuis) and to investigate the role of IgM cleavage in evasion of the classical complement pathway and pathogenesis. Targeted mutagenesis of a cysteine in the putative active center of IdeSsuis abrogated IgM cleavage completely. In contrast to wt rIdeSsuis, point mutated rIdeSsuis_C195S did not reduce complement-mediated hemolysis indicating that complement inhibition by rIdeSsuis depends on the IgM proteolytic activity. A S. suis mutant expressing IdeSsuis_C195S did not reduce IgM labeling, whereas the wt and complemented mutant showed less IgM F(ab’)2 and IgM Fc antigen on the surface. IgM cleavage increased survival of S. suis in porcine blood ex vivo and mediated complement evasion as demonstrated by blood survival and C3 deposition assays including the comparative addition of rIdeSsuis and rIdeSsuis_C195S. However, experimental infection of piglets disclosed no significant differences in virulence between S. suis wt and isogenic mutants without IgM cleavage activity. This work revealed for the first time in vivo labeling of S. suis with IgM in the cerebrospinal fluid of piglets with meningitis. In conclusion, this study classifies IdeSsuis as a cysteine protease and emphasizes the role of IgM cleavage for bacterial survival in porcine blood and complement evasion though IgM cleavage is not crucial for the pathogenesis of serotype 2 meningitis.

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“…The combination of MS methods facilitated the categorization of the interacting proteins into groups that specifically bind to the surface of S. pyogenes at high concentrations. Applying these methods to a strain that caused both asymptomatic pharyngitis and invasive disease within the same patient, 24 demonstrates the importance of interactions between S. pyogenes and human plasma proteins for the transition from mild to severe infection. The results also underline that the combination of mass spectrometry based techniques can improve our current understanding of molecular interactions that contribute to bacterial virulence, a knowledge that has the potential to identify novel opportunities to treat patients with invasive infections.…”

Section: Introductionmentioning

confidence: 99%

“…The results also underline that the combination of mass spectrometry based techniques can improve our current understanding of molecular interactions that contribute to bacterial virulence, a knowledge that has the potential to identify novel opportunities to treat patients with invasive infections. An M1 strain isolated from asymptomatic pharyngitis (in the throat) and from necrotic tissue (in the leg) of the same patient 24 was also investigated. Single colonies were grown to exponential phase in 30g/L Todd--Hewitt broth (BD) and 6g/L yeast extract (Merck, Darmstadt, Germany) (THY), harvested by centrifugation and resuspended in 20mM Tris--HCl(Merck), 150mM NaCl (Sigma--Aldrich, St. Louis, MO, USA), pH 7.6, to a concentration of 2x10 9 CFU/ml.…”

Section: Introductionmentioning

confidence: 99%

A comprehensive analysis of the Streptococcus pyogenes and human plasma protein interaction network

et al. 2014

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Link to publication Citation for published version (APA): Sjöholm, K., Karlsson, C., Linder, A., & Malmström, J. (2014). A comprehensive analysis of the Streptococcus pyogenes and human plasma protein interaction network. Molecular BioSystems, 10(7), 1698-1708. DOI: 10.1039/c3mb70555bGeneral rights Copyright and moral rights for the publications made accessible in the public portal are retained by the authors and/or other copyright owners and it is a condition of accessing publications that users recognise and abide by the legal requirements associated with these rights.• Users may download and print one copy of any publication from the public portal for the purpose of private study or research.• You may not further distribute the material or use it for any profit-making activity or commercial gain • You may freely distribute the URL identifying the publication in the public portal

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Antibody orientation at bacterial surfaces is related to invasive infection

Abstract: Bacterial surface proteins switch the orientation of IgG binding depending on the antibody concentration of their environment.

Cited by 99 publications

References 51 publications

Streptococcal Protein G Enhances Antibody Binding to Platinum Sensor Surfaces

Streptococcal Protein G Enhances Antibody Binding to Platinum Sensor Surfaces

IgM cleavage by Streptococcus suis reduces IgM bound to the bacterial surface and is a novel complement evasion mechanism

A comprehensive analysis of the Streptococcus pyogenes and human plasma protein interaction network

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