Binding of Fibrinogen Fragment D to Group A Streptococci Causes Strain Dependent Decrease in Cell Surface Hydrophobicity as Measured by the Salt Aggregation Test (SAT) and Cell Clumping in Polyethylene Glycol

Schmidt, Karl‐Hermann; Kühnemund, O; Wadström, Torkel

doi:10.1016/s0176-6724(87)80139-6

Cited by 4 publications

(7 citation statements)

References 19 publications

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“…Similar :294 results were obtained by Schmidt et al (72). Binding of the fibrinogen degradation products ~o the type 24 cocci appeared to be mediated by M protein, since PepM24 bound to fragments containing the terminal domains of the fibrinogen molecule, but not fragment E. PepM24 also inhrbited the binding of digested fibrinogen to streptococcal cells.…”

Section: Subsequent Studies By O'connor and Cleary-(63) D E M O N S Tsupporting

confidence: 78%

“…I m m u n ochemical techniques revealed the fibrinogen precipitating factor to be M protein. Subsequently, binding of fibrinogen and fibrinogen degradation products to group A streptococci have been dem o n s t r a t e d by several investigators (44,45,70,72,86). Whitnack and Beachey (85) have studied the role of fibrinogen for the phagocytosis-resistance of group A streptococci.…”

Section: Subsequent Studies By O'connor and Cleary-(63) D E M O N S Tmentioning

confidence: 99%

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Molecular aspects of the phagocytosis resistance of group a streptococci

Manjula

1988

Eur J Epidemiol

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Section: Subsequent Studies By O'connor and Cleary-(63) D E M O N S Tsupporting

confidence: 78%

Section: Subsequent Studies By O'connor and Cleary-(63) D E M O N S Tmentioning

confidence: 99%

Molecular aspects of the phagocytosis resistance of group a streptococci

Manjula

1988

Eur J Epidemiol

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“…It was of interest that binding of fibrinogen fragment D to M protein positive group A streptococci reduced the surface hydrophobicity of this strains. The latter could be demonstrated by an ammonium sulfate aggregation test (25). Surface hydrophobicities of In the present study this hexadecane adhesion test was used to measure surface hydrophobicity of streptococci of serological group B isolated from humans and bovines.…”

Section: Introductionmentioning

confidence: 95%

Relationship Between Group B Streptococcal Serotypes and Cell Surface Hydrophobicity

Wibawan

Lämmler

1992

Journal of Veterinary Medicine, Series B

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Cell surface hydrophobicities of streptococci of serological group B were determined by the adherence of the bacteria to hexadecane droplets. A significant adherence to hexadecane was observed with the group B streptococcal type reference strains Ib, V, Ic, Rand X, but not with those of serotype Ia, 11, 111 and IV. Cultivation of the bacteria in microcapsule-inducing media reduced the hexadecane adherence properties. The adherence to hexadecane was not related to fibrinogen binding properties of the cultures. Screening a large number of group B streptococci isolated from humans and bovines revealed that those with polysaccharide type antigen alone were generally hydrophilic, those with protein antigen alone or with protein antigen in combination with polysaccharide antigen were mostly hydrophobic. Cultivation of the bacteria under microaerobic conditions or after a single mouse passage enhanced microcapsule production and correspondingly reduced the hexadecane adherence values. Treatment of the bacteria by guanidinium chloride or by neuraminidase enhanced the hexadecane adherence. The hydrophobic component on group B streptococcal surface appeared to be partly inactivated by heat or proteolytic treatment of the bacteria. * Corresponding author. US. Copyright Clearance Center Code Statement: 093 1 -1793/92/3905 -0376$02.50/0 Relationship Between Group B Streptococcal Serotypes 377group A streptococci could also be determined by partition of the bacteria in an aqueous dextran polyethylene glycol two-phase system (13) and by the adherence of the bacteria to hexadecane droplets (19).

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“…In our laboratory we routinely check streptococcal isolates for expression of plasma protein binding proteins at the cell surface using a bacterial dot blot assay. Recent experiments revealed that such strains of GAS which bind fibrinogen and/or albumin at their cell surface mostly express proteins of the M family [29,31–33]. Fibrinogen binding seems to be a property of most M proteins [1,7,25,30–32,34] and contributes to the antiphagocytic properties of these cell surface proteins [29,33,42,43].…”

Section: Resultsmentioning

confidence: 99%

M protein of aStreptococcus dysgalactiaehuman wound isolate shows multiple binding to different plasma proteins and shares epitopes with keratin and human cartilage

Geyer

Röth

Vettermann

et al. 1999

FEMS Immunology &Amp; Medical Microbiology

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Besides group A (GAS), Lancefield group C beta-haemolytic streptococci (GCS) have been implicated as a causative agent in outbreaks of purulent pharyngitis. In this study we have investigated a class CI M protein of a Streptococcus dysgalactiae1:256, revealed that 26% of these sera showed serological cross-reactivity between a 68-kDa cartilage protein and the N-terminal part of MC. Only 8% of the sera of healthy patients showed this property. In additional, MC also cross-reacted with antibodies recognising epidermal keratins. The cross-reacting 68-kDa protein from cartilage was different from human serum albumin, but was recognised with anti-vimentin immune serum. The MC was cloned and the gene sequenced. By using PCR, recombinant gene fragments encoding characteristic peptide fragments of MC were expressed in Escherichia coli. The peptides were used to map the binding sites for plasma proteins and to locate the cross-reacting epitopes on the MC molecule. In consequence, sequence alignments revealed that MC shared homologous regions with vimentin and different keratins. Our data, obtained with MC, suggest that not only infections with GAS but also infections with GCS and possibly GGS (the latter species can also produce class CI M-like proteins) may be responsible for the formation of streptococcal-associated sequel diseases.

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Binding of Fibrinogen Fragment D to Group A Streptococci Causes Strain Dependent Decrease in Cell Surface Hydrophobicity as Measured by the Salt Aggregation Test (SAT) and Cell Clumping in Polyethylene Glycol

Cited by 4 publications

References 19 publications

Molecular aspects of the phagocytosis resistance of group a streptococci

Molecular aspects of the phagocytosis resistance of group a streptococci

Relationship Between Group B Streptococcal Serotypes and Cell Surface Hydrophobicity

M protein of aStreptococcus dysgalactiaehuman wound isolate shows multiple binding to different plasma proteins and shares epitopes with keratin and human cartilage

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