Comparative structure analysis of the multi-domain, cell envelope proteases of lactic acid bacteria

LF Christensen, MH Høie, CH Bang-Berthelsen… - Microorganisms, 2023 - mdpi.com
Lactic acid bacteria (LAB) have an extracellular proteolytic system that includes a multi-
domain, cell envelope protease (CEP) with a subtilisin homologous protease domain. These …

Impact of propeptide cleavage on the stability and activity of a streptococcal immunomodulatory C5a peptidase for biopharmaceutical development

V Gedi, F Duarte, P Patel, P Bhattacharjee… - Molecular …, 2023 - ACS Publications
Posttranslational modifications of proteins can impact their therapeutic efficacy, stability, and
potential for pharmaceutical development. The Group A Streptococcus pyogenes C5a …

[HTML][HTML] The protease associated (PA) domain in ScpA from Streptococcus pyogenes plays a role in substrate recruitment

S McKenna, F Aylward, X Miliara, RJ Lau… - … et Biophysica Acta (BBA …, 2023 - Elsevier
Annually, over 18 million disease cases and half a million deaths worldwide are estimated to
be caused by Group A Streptococcus. ScpA (or C5a peptidase) is a well characterised …

[HTML][HTML] An in-situ forming controlled release soft hydrogel-based C5a peptidase drug delivery system to treat psoriasis

P Patel, P Bhattacharjee, V Gedi, F Duarte… - International Journal of …, 2025 - Elsevier
The potent pro-inflammatory cytokine, interferon gamma (IFN-γ), is an enticing therapeutic
target because of its accelerator role in several acute and chronic inflammatory processes …

[HTML][HTML] C5a peptidase (ScpA) activity towards human type II and type III interferons

F Duarte, M Teçza, V Gedi, K McGourty, SP Hudson - Cytokine, 2024 - Elsevier
C5a peptidase, also known as ScpA, is a surface associated serine protease derived from
Streptococcus pyogenes and has been described as an important factor in streptococcus …

[HTML][HTML] Exosite binding modulates the specificity of the immunomodulatory enzyme ScpA, a C5a inactivating bacterial protease

M Jain, M Teçza, TF Kagawa, JC Cooney - Computational and Structural …, 2022 - Elsevier
The C5a peptidase from Streptococcus pyogenes (ScpA) is a highly specific enzyme with
potential therapeutic value. ScpA is a good model for studying determinants of specificity in …

The 1.7 Å crystal structure of the C5a peptidase from Streptococcus agalactiae (ScpB) reveals an active site competent for catalysis

R Cullen, M Teçza, T Miclot, S Behan… - Proteins: Structure …, 2024 - Wiley Online Library
A 1.7 Å structure is presented for an active form of the virulence factor ScpB, the C5a
peptidase from Streptococcus agalactiae. The previously reported structure of the ScpB …

Comparison of wild-type and codon-optimized Streptococcal cysteine protease SpeB expression in E. coli

N Miriyala - 2023 - researchrepository.ul.ie
Streptococcus pyogenes or group A streptococcus (GAS) is a Gram-positive bacteria known
to cause both mild and severe infections in humans. GAS strains secrete several proteases …

[HTML][HTML] X-ray diffraction data for the C5a-peptidase mutant with modified activity and specificity

TF Kagawa, M Jain, JC Cooney - Data in Brief, 2023 - Elsevier
The Streptococcal C5a peptidase (ScpA) specifically inactivates the human complement
factor hC5a, a potent anaphylatoxin recently identified as a therapeutic target for treatment of …