Proteolytic Processing, Maturation, and Unique Synteny of the Streptomyces Hemagglutinin SHA.

ABSTRACT: SHA is an l-rhamnose- and d-galactose-binding lectin that agglutinates human group B erythrocytes and was first purified almost 50 years ago. Although the original SHA-producing Streptomyces strain was lost, the primary structure of SHA was more recently solved by mass spectrometry of the archived protein, which matched it to a similar sequence in the Streptomyces lavendulae genome. Using genomic and protein biochemical analyses, this study aimed to identify SHA-secreting Streptomyces strains to further investigate the expression and binding activities of these putative proteins. Of 67 strains genetically related to S. lavendulae, 17 secreted pro-SHAs in culture. Seven SHA homologues were purified to homogeneity and then subjected to liquid chromatography-high-resoluti

SUBMITTER: Fujita-Yamaguchi Y 

PROVIDER: S-EPMC8557816 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature