Identification of group A type 1 streptococcal M protein gene by a non-radioactive oligonucleotide detection method

1990 ◽  
Vol 179 (5) ◽  
Author(s):  
Andreas Podbielski ◽  
Otto K�hnemund ◽  
Rudolf L�tticken
Keyword(s):  
Protein Gene ◽  
Detection Method ◽  
M Protein ◽  
Streptococcal M Protein ◽  
Group A ◽  
Oligonucleotide Detection

Interaction of Group A Type 1 Streptococcal M Protein With Fibrinogen

2009 ◽  
Vol 93B (1-6) ◽  
pp. 201-209
Author(s):  
O. Kühnemund ◽  
J. Havliček ◽  
H. Knöll ◽  
J. Sjöquist ◽  
W. Köhler
Keyword(s):  
M Protein ◽  
Streptococcal M Protein ◽  
Group A

scholarly journals Group A streptococcal M protein activates the NLRP3 inflammasome

2017 ◽  
Vol 2 (10) ◽  
pp. 1425-1434 ◽  
Author(s):  
J. Andrés Valderrama ◽  
Angelica M. Riestra ◽  
Nina J. Gao ◽  
Christopher N. LaRock ◽  
Naveen Gupta ◽  
...  
Keyword(s):  
Nlrp3 Inflammasome ◽  
M Protein ◽  
Streptococcal M Protein ◽  
Group A

scholarly journals Induction of human gamma interferon by structurally defined polypeptide fragments of group A streptococcal M protein.

1984 ◽  
Vol 43 (1) ◽  
pp. 122-126 ◽  
Author(s):  
D A Weigent ◽  
E H Beachey ◽  
T Huff ◽  
J W Peterson ◽  
G J Stanton ◽  
...  
Keyword(s):  
Gamma Interferon ◽  
M Protein ◽  
Streptococcal M Protein ◽  
Group A

scholarly journals Inhibition of the alternative C3 convertase and classical C5 convertase of complement by group A streptococcal M protein.

1990 ◽  
Vol 58 (8) ◽  
pp. 2535-2541 ◽  
Author(s):  
K Hong ◽  
T Kinoshita ◽  
J Takeda ◽  
H Kozono ◽  
P Pramoonjago ◽  
...  
Keyword(s):  
M Protein ◽  
Streptococcal M Protein ◽  
Group A

scholarly journals Structure-based group A streptococcal vaccine design: Helical wheel homology predicts antibody cross-reactivity among streptococcal M protein–derived peptides

2020 ◽  
Vol 295 (12) ◽  
pp. 3826-3836 ◽  
Author(s):  
Michelle P. Aranha ◽  
Thomas A. Penfound ◽  
Jay A. Spencer ◽  
Rupesh Agarwal ◽  
Jerome Baudry ◽  
...  
Keyword(s):  
Group A Streptococcus ◽  
Coiled Coil ◽  
Cross Reactivity ◽  
M Protein ◽  
High Sequence Identity ◽  
Sequence Identity ◽  
Streptococcal M Protein ◽  
Helical Wheel ◽  
Group A ◽  
Immunological Assays

Group A streptococcus (Strep A) surface M protein, an α-helical coiled-coil dimer, is a vaccine target and a major determinant of streptococcal virulence. The sequence-variable N-terminal region of the M protein defines the M type and also contains epitopes that promote opsonophagocytic killing of streptococci. Recent reports have reported considerable cross-reactivity among different M types, suggesting the prospect of identifying cross-protective epitopes that would constitute a broadly protective multivalent vaccine against Strep A isolates. Here, we have used a combination of immunological assays, structural biology, and cheminformatics to construct a recombinant M protein–based vaccine that included six Strep A M peptides that were predicted to elicit antisera that would cross-react with an additional 15 nonvaccine M types of Strep A. Rabbit antisera against this recombinant vaccine cross-reacted with 10 of the 15 nonvaccine M peptides. Two of the five nonvaccine M peptides that did not cross-react shared high sequence identity (≥50%) with the vaccine peptides, implying that high sequence identity alone was insufficient for cross-reactivity among the M peptides. Additional structural analyses revealed that the sequence identity at corresponding polar helical-wheel heptad sites between vaccine and nonvaccine peptides accurately distinguishes cross-reactive from non–cross-reactive peptides. On the basis of these observations, we developed a scoring algorithm based on the sequence identity at polar heptad sites. When applied to all epidemiologically important M types, this algorithm should enable the selection of a minimal number of M peptide–based vaccine candidates that elicit broadly protective immunity against Strep A.

scholarly journals A local α-helix drives structural evolution of streptococcal M-protein affinity for host human plasminogen

2020 ◽  
Vol 477 (9) ◽  
pp. 1613-1630
Author(s):  
Cunjia Qiu ◽  
Yue Yuan ◽  
Shaun W. Lee ◽  
Victoria A. Ploplis ◽  
Francis J. Castellino
Keyword(s):  
Tight Binding ◽  
Class Ii ◽  
Class I ◽  
M Protein ◽  
Class Iii ◽  
Streptococcal M Protein ◽  
Special Cases ◽  
Group A ◽  
Human Plasminogen ◽  
A Domains

Plasminogen-binding group A streptococcal M-protein (PAM) is a signature surface virulence factor of specific strains of Group A Streptococcus pyogenes (GAS) and is an important tight binding protein for human plasminogen (hPg). After activation of PAM-bound hPg to the protease, plasmin (hPm), GAS cells develop invasive surfaces that are critical for their pathogenicity. PAMs are helical dimers in solution, which are sensitive to temperature changes over a physiological temperature range. We previously categorized PAMs into three classes (I–III) based on the number and nature of short tandem α-helical repeats (a1 and a2) in their NH2-terminal A-domains that dictate interactions with hPg/hPm. Class II PAMs are special cases since they only contain the a2-repeat, while Class I and Class III PAMs encompass complete a1a2-repeats. All dimeric PAMs tightly associate with hPg, regardless of their categories, but monomeric Class II PAMs bind to hPg much weaker than their Class I and Class III monomeric counterparts. Additionally, since the A-domains of Class II PAMs comprise different residues from other PAMs, the issue emerges as to whether Class II PAMs utilize different amino acid side chains for interactions with hPg. Herein, through NMR-refined structural analyses, we elucidate the atomic-level hPg-binding mechanisms adopted by two representative Class II PAMs. Furthermore, we develop an evolutionary model that explains from unique structural perspectives why PAMs develop variable A-domains with regard to hPg-binding affinity.

Sign in / Sign up

Export Citation Format

Share Document