scholarly journals Selective Distribution of a High-Affinity Plasminogen-Binding Site among Group A Streptococci Associated with Impetigo

1999 ◽  
Vol 67 (8) ◽  
pp. 3915-3920 ◽  
Author(s):  
Mikael D. Svensson ◽  
Ulf Sjöbring ◽  
Debra E. Bessen
Keyword(s):  
Binding Site ◽  
Plasma Proteins ◽  
Surface Proteins ◽  
Gene Marker ◽  
Site Preference ◽  
Group A Streptococci ◽  
High Affinity ◽  
High Affinity Binding Site ◽  
Group A ◽  
Tissue Site

ABSTRACT Group A streptococci can be classified according to their tendency to cause either impetigo, pharyngitis, or both types of infection. Genotypic markers for tissue site preference lie within emmgenes, which encode fibrillar surface proteins that play a key role in virulence. emm gene products (M and M-like proteins) display an extensive array of binding activities for tissue and plasma proteins of the human host. In a previous study, a high-affinity binding site for human plasmin(ogen) was mapped to theemm53 gene product. In this report, a structurally similar plasminogen-binding domain is found to be widely and selectively distributed among group A streptococci harboring the emmgene marker for the skin as the preferred tissue site for infection. The findings are highly suggestive of a central role for bacterial modulation of host plasmin(ogen) during localized infection at the epidermis.

scholarly journals High-affinity binding site for a specific nuclear protein in the human IgM gene

Nature ◽  
1985 ◽  
Vol 315 (6016) ◽  
pp. 254-254
Author(s):  
L. Hennighausen ◽  
U. Siebenlist ◽  
D. Danner ◽  
P. Leder ◽  
D. Rawlins ◽  
...  
Keyword(s):  
Binding Site ◽  
Nuclear Protein ◽  
Affinity Binding ◽  
High Affinity Binding ◽  
High Affinity ◽  
High Affinity Binding Site ◽  
Specific Nuclear Protein

The Amino Acid Sequence in Fibrin Responsible for High Affinity Thrombin Binding

2001 ◽  
Vol 85 (03) ◽  
pp. 470-474 ◽  
Author(s):  
Kevin Siebenlist ◽  
Stephen Brennan ◽  
Trudy Holyst ◽  
Michael Mosesson ◽  
David Meh
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Binding Site ◽  
Binding Affinity ◽  
Ionization Mass ◽  
Consensus Sequences ◽  
High Affinity ◽  
High Affinity Binding Site ◽  
Carboxy Terminal ◽  
Sulfated Peptides

SummaryHuman fibrin has a low affinity thrombin binding site in its E domain and a high affinity binding site in the carboxy-terminal region of its variant ’ chain (’408-427). Comparison of the ’ amino acid sequence (VRPEHPAETEYDSLYPEDDL) with other protein sequences known to bind to thrombin exosites such as those in GPIb , the platelet thrombin receptor, thrombomodulin, and hirudin suggests no homology or consensus sequences, but Glu and Asp enrichment are common to all. Tyrosine sulfation in these sequences enhances thrombin exosite binding, but this has not been uniformly investigated. The fibrinogen ’ chain mass determined by electrospray ionization mass spectrometry, was 50,549 Da, a value 151 Da greater than predicted from its amino acid/carbohydrate sequence. Since each sulfate group increases mass by 80 Da, this indicates that both tyrosines at 418 and 422 are sulfated. A series of overlapping ’ peptides was prepared for evaluation of their inhibition of 125I-labeled PPACK-thrombin binding to fibrin. ’414-427 was as effective an inhibitor as ’408-427 and its binding affinity was dependent on all carboxy-terminal residues. Mono Tyr-sulfated peptides were prepared by substituting non-sulfatable Phe for Tyr at ’ 418 or 422. Sulfation at either Tyr residue increased binding competition compared with non-sulfated peptides, but was less effective than doubly sulfated peptides, which had 4 to 8-fold greater affinity. The reverse ’ peptide or the forward sequence with repositioned Tyr residues did not compete well for thrombin binding, indicating that the positions of charged residues are important for thrombin binding affinity

Regulatory effect of cholecystokinin on subsequent insulin binding to pancreatic acini

1990 ◽  
Vol 258 (4) ◽  
pp. E562-E568
Author(s):  
Y. Okabayashi ◽  
M. Otsuki ◽  
T. Nakamura ◽  
M. Koide ◽  
H. Hasegawa ◽  
...  
Keyword(s):  
Binding Site ◽  
Insulin Binding ◽  
Pancreatic Acinar Cells ◽  
Affinity Binding ◽  
Regulatory Effect ◽  
Pancreatic Acini ◽  
High Affinity Binding ◽  
Receptor Affinity ◽  
High Affinity ◽  
High Affinity Binding Site

We investigated the regulatory effect of cholecystokinin (CCK) on subsequent insulin binding to pancreatic acinar cells. Rat isolated acini were preincubated with various concentrations of CCK octapeptide (CCK-8) at 37 degrees C. Acini were then washed, resuspended in the binding buffer, and incubated with 8.3 pM 125I-labeled insulin for 60 min at 37 degrees C. Pretreatment with CCK-8 caused inhibition of subsequent 125I-insulin binding that was time and concentration dependent. Significant inhibition was observed with 3 pM CCK-8. Computer analysis of the competition-inhibition study with a nonlinear least-squares curve-fitting program revealed that CCK-8 pretreatment of acini reduced the receptor affinity of the high-affinity binding site. This inhibitory action of CCK-8 was not due to the alteration in degradation or internalization of the tracer. When acini were pretreated with 100 pM CCK-8 for 120 min at 4 degrees C, a reduction in the receptor affinity of the high-affinity binding site was also observed. In pancreatic membrane prepared from acini preincubated with 100 pM CCK-8 for 120 min at 37 degrees C, displacement of 125I-insulin (83 pM) by unlabeled insulin (24 degrees C, 1 h) revealed that CCK-8 inhibited 125I-insulin binding by altering the receptor affinity of the high-affinity binding site. In acinar preparations the inhibitory effect of CCK-8 on 125I-insulin binding was abolished when acini were preincubated with CCK-8 and CCK receptor antagonist L 374718 at 37 degrees C.(ABSTRACT TRUNCATED AT 250 WORDS)

A gonadotropin-releasing hormone type neuropeptide with a high affinity binding site for copper(ii) and nickel(ii)

Metallomics ◽  
2019 ◽  
Vol 11 (2) ◽  
pp. 404-414 ◽  
Author(s):  
Kevin K. Tran ◽  
Bhawantha M. Jayawardena ◽  
Maurice R. Elphick ◽  
Christopher E. Jones
Keyword(s):  
Binding Site ◽  
Gonadotropin Releasing Hormone ◽  
Affinity Binding ◽  
Asterias Rubens ◽  
High Affinity Binding ◽  
Releasing Hormone ◽  
High Affinity ◽  
Evolutionarily Conserved ◽  
High Affinity Site ◽  
High Affinity Binding Site

Gonadotropin releasing hormone from Asterias rubens binds Cu(ii) in a nitrogen-rich, high-affinity site. Cu(ii)-binding is an evolutionarily conserved feature of GnRH-type neuropeptides.

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