RT Journal Article SR Electronic(1) A1 Winram, Scott B. A1 Lottenberg, RichardYR 1996 T1 The plasmin-binding protein Plr of group A streptococci is identified as glyceraldehyde-3-phosphate dehydrogenase JF Microbiology, VO 142 IS 8 SP 2311 OP 2320 DO https://doi.org/10.1099/13500872-142-8-2311 PB Microbiology Society, SN 1465-2080, AB Group A streptococci bind the serine protease plasmin with high affinity. Previously, a 41 kDa protein was identified as a candidate plasmin receptor protein (Plr) from group A streptococcal strain 64/14. The plr gene encoding Plr was cloned and the deduced amino acid sequence of Plr had significant similarity to glyceraldehyde-3-phosphate dehydrogenases (GAPDHs). In this study we have isolated cytoplasmic GAPDH of streptococcal strain 64/14. This enzyme was examined, on both structural and functional levels, for its relatedness to the Plr of strain 64/14 purified from mutanolysin extract and to recombinant Plr. We report here that no differences were detected between streptococcal Plr and cytoplasmic GAPDH on the basis of antibody reactivity, plasmin-binding activity, GAPDH activity, N-terminal amino acid sequence, peptide map analysis by V8 protease digestion and amino acid composition analysis. Furthermore, the plr gene appears to be present as a single copy in group A streptococci., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/13500872-142-8-2311