Molecular analysis of Streptococcus anginosus-derived SagA peptides.

Abstract:

BACKGROUND:SagA1 and SagA2 molecules produced from beta-hemolytic Streptococcus anginosus subsp. anginosus are composed of a leader peptide and a propeptide, and their mature form has hemolytic activity as a well-known Streptococcal peptide toxin, streptolysin. The function of these SagA molecules is thought to be dependent on intra-molecular heterocycle formation. In this study, we examined the heterocycle-involved molecular features of SagA1, SagA2, and S. pyogenes SagA (SPySagA), focusing on their heterocycle formation. MATERIALS AND METHODS:Molecular models of SagA1, SagA2, and SPySagA were constructed using a molecular modeling technique. Molecular dynamics and molecular mechanic analyses of the modeled SagA molecules were performed to obtain their energy profiles. RESULTS:Total energy of the modeled SagA1, SagA2, and SPySagA decreased with heterocycle formation, and the border between the leader peptide and propeptide was clearly observed after heterocycle formation. CONCLUSION:The flexibility of SagA molecules was changed by intramolecular heterocycle formation, and their function (e.g. hemolytic activity) seems to be regulated by structural transition with heterocycle formation.

journal_name

Anticancer Res

journal_title

Anticancer research

authors

Kawaguchi Y,Tabata A,Nagamune H,Ohkura K

subject

Has Abstract

pub_date

2014-08-01 00:00:00

pages

4627-31

issue

8

eissn

0250-7005

issn

1791-7530

pii

34/8/4627

journal_volume

34

pub_type

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