Recombinant Yersinia pseudotuberculosis serotype O:1b Bifunctional protein aas (aas)
Description
Virulence Factors and Mechanisms
Yersinia species, including Y. pseudotuberculosis, harbor a 70-kb virulence plasmid that enables them to survive and multiply within the host's lymphoid system . This plasmid encodes for Yop (Yersinia outer proteins) effectors, which are crucial for the bacteria's pathogenicity. Several Yops, such as YopE and YopH, act in concert to inhibit phagocytosis by macrophages, allowing Yersinia to proliferate in Peyer’s patches as extracellular microcolonies .
Yersinia can resist specific uptake via Fc receptors, and pretreatment with wild-type bacteria can block a general phagocytic mechanism . Furthermore, Yersinia inhibits the release of tumor necrosis factor-alpha (TNF-α) by macrophages, requiring a functional type III secretion machinery, a Yop translocation apparatus, and the effector YopP (Y. enterocolitica)/YopJ (Y. pseudotuberculosis) .
O-Specific Polysaccharide (OPS) Structure
The O-specific polysaccharide (OPS) is a crucial component of the lipopolysaccharide (LPS) in Gram-negative bacteria like Yersinia . The OPS of Y. pseudotuberculosis serotype O:15, for example, has a pentasaccharide repeating unit with a tetrameric backbone identical to that of O:5a and a branching paratofuranose residue identical to that of O:1b .
Table 1: 1H and 13C Chemical Shifts (δ) of the OPS from Y. pseudotuberculosis O:15
| Residue | H-/C-1 | H-/C-2 | H-/C-3 | H-/C-4 | H-/C-5 | H-/C-6 |
|---|---|---|---|---|---|---|
| A !3)-α-D-GalpNAc | 5.29 | 4.40 | 3.88 | 4.02 | 4.20 | 3.78–3.73 |
| B α-D-Asc | ||||||
| C α-L-Fucp | ||||||
| D →2)-α-D-Manp |
The O:15 structure contains a tetrameric backbone identical to that of O:5a, while the branching paratofuranose residue is identical to that of O:1b. The enzymes necessary for the biosynthesis of the O:15 repeating unit are encoded by a gene cluster, which also handles translocation and polymerization into OPS .
Role of Metallo-Oligopeptidase OpdA
Oligopeptidases, such as OpdA in Y. pseudotuberculosis, are involved in the degradation of short peptides and leader peptides released during protein secretion . OpdA is required for bacterial virulence, and its enzymatic activity is dependent on divalent cations .
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Zn2+ stimulates activity at low concentrations but inhibits it at higher concentrations.
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Co2+, Ca2+, and Mn2+ stimulate activity at all concentrations tested.
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Mg2+ has no effect on enzyme activity.
Product Specs
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Target Background
This bifunctional protein plays a critical role in lysophospholipid acylation. Specifically, it catalyzes the transfer of fatty acids to the 1-position of lysophospholipids via an enzyme-bound acyl-ACP intermediate. This process requires ATP and magnesium ions. Its physiological function is the regeneration of phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE), a byproduct of transacylation reactions or phospholipase A1 degradation.
KEGG: ypi:YpsIP31758_0975
