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TitleMechanism and inhibition of Streptococcus pneumoniae IgA1 protease.
Journal, issue, pagesNat Commun, Vol. 11, Issue 1, Page 6063, Year 2020
Publish dateNov 27, 2020
AuthorsZhiming Wang / Jeremy Rahkola / Jasmina S Redzic / Ying-Chih Chi / Norman Tran / Todd Holyoak / Hongjin Zheng / Edward Janoff / Elan Eisenmesser /
PubMed AbstractOpportunistic pathogens such as Streptococcus pneumoniae secrete a giant metalloprotease virulence factor responsible for cleaving host IgA1, yet the molecular mechanism has remained unknown since ...Opportunistic pathogens such as Streptococcus pneumoniae secrete a giant metalloprotease virulence factor responsible for cleaving host IgA1, yet the molecular mechanism has remained unknown since their discovery nearly 30 years ago despite the potential for developing vaccines that target these enzymes to block infection. Here we show through a series of cryo-electron microscopy single particle reconstructions how the Streptococcus pneumoniae IgA1 protease facilitates IgA1 substrate recognition and how this can be inhibited. Specifically, the Streptococcus pneumoniae IgA1 protease subscribes to an active-site-gated mechanism where a domain undergoes a 10.0 Å movement to facilitate cleavage. Monoclonal antibody binding inhibits this conformational change, providing a direct means to block infection at the host interface. These structural studies explain decades of biological and biochemical studies and provides a general strategy to block Streptococcus pneumoniae IgA1 protease activity to potentially prevent infection.
External linksNat Commun / PubMed:33247098 / PubMed Central
MethodsEM (single particle)
Resolution3.8 - 4.8 Å
Structure data

22204

6xja

EMDB-22204, PDB-6xja:
Streptococcus Pneumoniae IgA1 Protease with IgA1 substrate
Method: EM (single particle) / Resolution: 4.0 Å

22205

6xjb

EMDB-22205, PDB-6xjb:
IgA1 Protease
Method: EM (single particle) / Resolution: 3.8 Å

22328

7jgj

EMDB-22328, PDB-7jgj:
IgA1 Protease in complex with neutralizing mAb
Method: EM (single particle) / Resolution: 4.8 Å

Source
  • streptococcus pneumoniae (strain atcc baa-255 / r6) (bacteria)
  • homo sapiens (human)
  • Human (human)
  • streptococcus pneumoniae (bacteria)
  • mus musculus (house mouse)
KeywordsIMMUNE SYSTEM / IgA1 / Complex / Protease / metalloprotease / neutralization

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