Fix label and definiton GO:0044542 'plasminogen activation in another organism'

[pgaudet]

For the GO-PathGO alignment, we will

• [x] change the label of GO:0044542 'plasminogen activation in another organism' to GO:0044542 symbiont-mediated activation of host plasminogen
• [x] change the definition to "A process in which a symbiont initiates, promotes, or enhances the normal activation of plasminogen, the pathway resulting in the processing of inactive plasminogen to active plasmin in the host organism."
• [x] move term under GO:0044003 'modulation by symbiont of host process'

@genegodbold to provide references and also to look into whether this is the same or one mechanism for complement inhibition? ie it could perhaps be a child of 'symbiont-mediated suppression of host complement activation'

current children are:

• 'symbiont-mediated suppression of host complement activation by complement sequestering'
• 'symbiont-mediated suppression of host complement activation by inactivation of complement proteins'
• 'symbiont-mediated suppression of host complement activation by recruitment of complement control protein'

[genegodbold]

Gene's summary: Bound plasminogen converted to plasmin allows bacteria to disseminate into tissues. It also is used to destroy complement (and opsonins) as well as antibacterial proteins like histones.

This is just a handful of plasminogen binding proteins from bacteria. I've annotated dozens.

• Endopeptidase O (PepO; Neprilysin) from Streptococcus suis: SsPepO binds host fibronectin [PMID:29253192]. SsPepO is a plasminogen-binding protein as assessed using ELISA plates coated with increasing concentrations of plasminogen. The fibronectin and plasminogen binding sites on SsPepO are independent of one another. SsPepO facilitates the attachment of the bacterium to plasminogen and enables adherence and invasion into rat brain microvessel endothelial cells. This is significant because Streptococcus suis is one of the causes of meningitis. Host plasminogen bound to SsPepO can be converted to plasmin via proteolysis by host uPA and can then degrade host complement C3b and enabling the control of complement activation. A bacterial mutant lacking PepO has impaired adherence to plasminogen, invasion of rat brain microvessel endothelial cells, and is efficiently killed by human serum and blood [PMID:34305859].
• Streptokinase from Streptococcus pyogenes: Streptokinase is a host plasminogen activator generating the serine protease plasmin [PMID:15972548]. Streptokinase hijacks the host fibrinolytic system to generate plasmin that can overcome defensive fibrin barriers thrown together by the host. On this account, streptokinase is a dissemination factor [PMID:28125743]. Host histones are antibacterial and hemolytic and complement the innate immune system in the formation of neutrophil extracellular traps (NETs) in defeating bacterial parasites. Streptococcus pyogenes protects itself from histone-killing by the acquisition of plasminogen. Plasminogen bound to the streptococcal surface via streptokinase protects the bacterial cell from histone-mediated killing. The streptokinase-plasminogen complex degrades all classes of histones and abrogates their antibacterial and hemolytic effects [PMID:27533300].
• Choline binding protein E (CbpE) from Streptococcus pneumoniae: The phosphorylcholine esterase domain of CbpE interacts with the kringle domains of host plasminogen. Plasminogen bound to the surface of the streptococcal bacterium allows its activation to plasmin. CbpE-bound plasmin allowed the pneumococcus to disseminate across the extracellular matrix in an in vitro model [PMID:18070889].
• Plasminogen surface receptor (hPg/hPm-binding M-protein; plasminogen binding groupA streptococcal M-like protein; PAM; antiphagocytic M protein; fibronectin binding protein; MRP4 protein; Ig-binding protein) from Streptococcus: Human factor H is recruited to the streptococcal surface by PAM along with human plasminogen/plasmin. These contribute to the degradation of the opsonin human C3b to its inactive product (iC3b), protecting the bacterium from phagocytosis. Factor H and factor I cleave C3b while plasmin cuts iC3b into smaller peptides [PMID:26945067].
• Staphylokinase from Staphylococcus aureus: Secreted SAK promotes the establishment of skin infections in humans and increases bacterial penetration through skin barriers by activating plasminogen but it does not promote systemic dissemination [PMID:23801604]. SAK is anti-opsonic, inhibiting S_aureus from being phagocytosed by host neutrophils in vitro. S_aureus has several plasminogen-binding receptors at the cell surface which bind host plasminogen. Surface bound plasminogen can be activated into the active plasmin protease by SAK on the surface of the bacterium. This allows the surface-bound plasmin to cleave both immunoglobulin G (IgG) and the complement proteins C3b and C3bi, thus inhibiting bacterial destruction by complement. Thus SAK activation of bacteria-bound host plasminogen to plasmin on the bacterial surface protects the bacterium from host defenses [PMID:15792635].
• Leptospiral elongation factor-Tu can be found on the bacterial surface where it binds plasminogen in a dose-dependent manner. The plasminogen is converted to plasmin which can cut host complement component C3b as well as fibrinogen. EF-Tu can also bind the host complement regulator factor H which can mediated C3b degradation by host Factor I. Thus EF-Tu can protect the bacterium from complement-mediated destruction [PMID:24312361].