Isolation and properties of a novel IgG-binding protein from streptococci of serological group U

Chhatwal, Gursharan S.; Blobel, H.

doi:10.1007/bf00189403

Cited by 10 publications

(4 citation statements)

References 23 publications

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“…Several interactions of host plasma proteins with certain pathogenic bacteria have been described previously (3,5,8,20,22,27). There is evidence that the binding of host proteins to bacteria plays a role in the pathogenicity of the bacteria (3,51).…”

Section: Discussionmentioning

confidence: 94%

Specific binding of the human S protein (vitronectin) to streptococci, Staphylococcus aureus, and Escherichia coli

Chhatwal¹,

Preissner²,

Müller‐Berghaus³

et al. 1987

Infect Immun

205

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Specific binding of the 1251-labeled human S protein (vitronectin) which has been shown to be identical with serum-spreading factor, was observed with group A, C, and G streptococci as well as with Staphylococcus aureus and Escherichia coli. The specific binding of S protein to group A, C, and G streptococci was high, whereas the binding to S. aureus and E. coli cultures was moderate. In contrast, group B streptococci and a number of other bacterial species tested did not interact with S protein. The binding of S protein to bacteria was saturable and could be inhibited only by unlabeled S protein but not by albumin. Trypsinization and heat treatment of bacteria destroyed the S-protein binding capacity for group G streptococci, S. aureus, and E. coli but not for group A and C streptococci. Likewise, unlabeled human fibronectin and heparin inhibited the binding of labeled S protein to group G streptococci, S. aureus, and E. coli, but did not influence the binding to group A and C streptococci. Double-reciprocal plots of S-protein binding to group G streptococci indicated that fibronectin inhibited the binding in a, competitive manner, while heparin acts in a noncompetitive manner. Moreover, the binding of S protein to G streptococci could be partially inhibited by the synthetic peptide Gly-Arg-Gly-Asp-Ser, which contains the cell attachment site of S protein. Trypsin-treated S protein had similar binding activity as untreated S protein for group G streptococci, S. aureus, and E. coli, but showed reduced binding to group A and C streptococci. The present data are indicative of two different types of bacterial binding sites in S protein. The binding to group G streptococci, S. aureus, and E. coli is mediated in part through a domain in the S protein containing the sequence Arg-Gly-Asp, whereas a different site is responsible for the binding to group A and C streptococci.

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Section: Discussionmentioning

confidence: 94%

Specific binding of the human S protein (vitronectin) to streptococci, Staphylococcus aureus, and Escherichia coli

Chhatwal¹,

Preissner²,

Müller‐Berghaus³

et al. 1987

Infect Immun

205

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“…c2M-trypsin complex (c2M-T) was prepared by the method of Kaplan and Nielson (14), and a2M-methylamine complex (a2M-M) was prepared as described by Osterberg and Malmensten (22). a2M, C2M-T, and a2M-M were radiolabeled by the chloramine T method as described previously (3,4). The specific activities were 1.2 mCi/mg for cx2M, 0.9 mCi/mg for t2M-T, and 1.0 mCi/mg for ot2M-M.…”

Section: Methodsmentioning

confidence: 99%

Novel complex formed between a nonproteolytic cell wall protein of group A streptococci and alpha 2-macroglobulin

Chhatwal¹,

Albohn²,

Blobel³

1987

J Bacteriol

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Binding of 125I-labeled alpha 2-macroglobulin (alpha 2M) to streptococci belonging to serological groups A, B, C, and G was studied. Streptococci of groups A and G interacted only with native alpha 2M, and those of group C reacted only with alpha 2M-trypsin complex. Binding of alpha 2M to group A streptococci was saturable and reversible. The dissociation constant was 2.02 X 10(-7) M, and the number of binding sites was calculated to be 18,000 per streptococcus. The alpha 2M-binding protein could be solubilized by treatment of group A streptococci with a murolytic enzyme and subsequently purified by affinity chromatography and high-pressure liquid chromatography. The purified protein was homogeneous on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and had a molecular weight of 78,000. It possessed no proteolytic activity and interacted with native alpha 2M in Western blots (immunoblots). Interaction of purified binding protein with alpha 2M led to a change in the conformation of alpha 2M similar to that obtained by alpha 2M-protease complexes. Reversible binding of a nonproteolytic streptococcal component of alpha 2M is thus a novel feature of alpha 2M reactivity.

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“…The lysate was centrifuged for 30 min at 10000 x g to remove unlyzed cells. The supernatant was dialyzed against phosphate buffered saline (PBS) and applied to a fibrinogen-Sepharose (1.2 x 15 cm) which was prepared in the same way as the preparation of IgG-Sepharose described previously [12]. After washing the column with PBS, the bound clumping factor was eluted with 0.2 M glycine-HC1 buffer, pH 2.5.…”

Section: Purification Of Clumping Factormentioning

confidence: 99%

“…Purity and molecular weight of clumping factor preparation was determined by SDS-PAGE [13] with 12% gels using a Protean II cell (Biorad, Munich, F.R.G.). For western blotting the proteins in SDS-PAGE gels were transferred to nitrocellulose membrane [12]. After saturation of unoccupied sites with 10% skimmed milk, the membranes were treated with fibrinogen or fibronectin and subsequently with peroxidase labelled anti-human fibrinogen or anti-human fibronectin antibodies [14].…”

Section: Sds-pa Ge and Western Blottingmentioning

confidence: 99%

Interaction between fibronectin and purified staphylococcal clumping factor

Chhatwal

1987

FEMS Microbiology Letters

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Isolation and properties of a novel IgG-binding protein from streptococci of serological group U

Cited by 10 publications

References 23 publications

Specific binding of the human S protein (vitronectin) to streptococci, Staphylococcus aureus, and Escherichia coli

Specific binding of the human S protein (vitronectin) to streptococci, Staphylococcus aureus, and Escherichia coli

Novel complex formed between a nonproteolytic cell wall protein of group A streptococci and alpha 2-macroglobulin

Interaction between fibronectin and purified staphylococcal clumping factor

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