This recombinant Staphylococcus aureus Zinc metalloproteinase aureolysin (aur) is a semi-custom product. There are 5 expression system options: Yeast, E. coli, In Vivo Biotinylation in E. coli, Baculovirus, and Mammalian cell. Your requirements will be given top priority in determining the protein tags. For proteins within 800 aa, risk-free custom service is guaranteed. It means you will not be charged if the protein cannot be delivered.
Aureolysin is a zinc-dependent metalloenzyme that requires both zinc and calcium ions for its activity [1][2][3]. It is the only metalloprotease produced by S. aureus and belongs to the family of thermolysins [4]. Aureolysin plays a significant role in S. aureus virulence by cleaving complement C3 to mediate immune evasion [5]. Additionally, aureolysin is involved in degrading human antimicrobial peptides, such as LL-37, which contributes to S. aureus resistance to host defenses [6]. It has been identified as a potential target for combating methicilin-resistant S.aureus.
Aureolysin's activity is essential for S. aureus growth on host proteins under nutrient-limited conditions, highlighting its role in bacterial survival and proliferation [7]. Furthermore, aureolysin has been implicated in modulating bone remodeling during osteomyelitis, showcasing its impact on bone infections caused by S. aureus.
References:
[1] A. Banbula, J. Potempa, J. Travis, C. Fernandez-Catalén, K. Mann, R. Huberet al., Amino-acid sequence and three-dimensional structure of the staphylococcus aureus metalloproteinase at 1.72 å resolution, Structure, vol. 6, no. 9, p. 1185-1193, 1998. https://doi.org/10.1016/s0969-2126(98)00118-x
[2] M. A, Role of extracellular proteases in biofilm disruption of gram positive bacteria with special emphasis on staphylococcus aureus biofilms, Enzyme Engineering, vol. 04, no. 01, 2014. https://doi.org/10.4172/2329-6674.1000126
[3] A. Laarman, M. Ruyken, C. Malone, J. Strijp, A. Horswill, & S. Rooijakkers, staphylococcus aureus metalloprotease aureolysin cleaves complement c3 to mediate immune evasion, The Journal of Immunology, vol. 186, no. 11, p. 6445-6453, 2011. https://doi.org/10.4049/jimmunol.1002948
[4] M. Sieprawska-Lupa, P. Mydel, K. Krawczyk, K. Wójcik, M. Puklo, B. Lupaet al., Degradation of human antimicrobial peptide ll-37 by staphylococcus aureus-derived proteinases, Antimicrobial Agents and Chemotherapy, vol. 48, no. 12, p. 4673-4679, 2004. https://doi.org/10.1128/aac.48.12.4673-4679.2004
[5] M. Lehman, A. Nuxoll, K. Yamada, T. Kielian, S. Carson, & P. Fey, Protease-mediated growth of staphylococcus aureus on host proteins is
opp3 dependent, Mbio, vol. 10, no. 2, 2019. https://doi.org/10.1128/mbio.02553-18
[6] J. Cassat, N. Hammer, J. Campbell, M. Benson, D. Perrien, L. Mraket al., A secreted bacterial protease tailors the staphylococcus aureus virulence repertoire to modulate bone remodeling during osteomyelitis, Cell Host & Microbe, vol. 13, no. 6, p. 759-772, 2013. https://doi.org/10.1016/j.chom.2013.05.003
[7] Y. Elhakim, A. Ali, A. Hosny, & N. Abdeltawab, Zinc deprivation as a promising approach for combating methicillin-resistant staphylococcus aureus: a pilot study, Pathogens, vol. 10, no. 10, p. 1228, 2021. https://doi.org/10.3390/pathogens10101228
