Table 1: Bacterial plasminogen receptors and their interactions with plasminogen.

Plasminogen receptorBacterial species Cell surface attachmentBinding affinity ( 𝐾 𝐷 )Binding interactions and characteristicsReferences

Bfp60Bacteroides fragilisAnchoredNDND[42]
Choline-binding protein E (CBPE)Streptococcus pneumoniaeAnchoredNDBinds plg via internal lysine residues K259, K267, and K319 present in the phosphorylcholine esterase domain.[43, 44]
CRASP-1, 3, 4, and 5Borrelia burgdorferiAnchoredNDND[45]
ErpP, ErpC, and ErpABorrelia burgdorferiAnchoredGlu-plg: 𝐾 𝐷 = 25 nMPlg binding is associated with C-terminal lysine residues. Bound plg can be activated by uPA.[46]
Erp63Borrelia spielmaniiAnchoredNDND[47]
FlagellaEscherichia coliAnchoredNDND[48]
GlnA1Mycobacterium tuberculosisAnchoredNDInteract with LBS within plg [49]
LenALeptospira interogansAnchoredNDInteracts with the K1–K3 plg fragment[46, 50]
Leptospiral surface adhesin Lsa66Leptospira interrogansAnchoredPlg: 𝐾 𝐷 = 68.8 nMND. Bound plg can be activated by uPA[51]
Lp30Leptospira interrogansAnchoredPlg: 𝐾 𝐷 = 167.39 nMND. Bound plg can be activated by uPA[51]
Leptospira interrogansAnchored  Plg: 𝐾 𝐷 = 11.97 nM
Plg: 𝐾 𝐷 = 10.98 nM
ND. Bound plg can be activated by uPA[52]
LipL32, LipL40Leptospira interrogansAnchoredND[52]
Lp29, Lp49Leptospira interrogansAnchoredND[52]
Leptospira interrogansAnchoredND
Plg: 𝐾 𝐷 = 68.8 nM
Streptococcus pyogenesGlu-plg: 𝐾 𝐷 = 1.6 nM–7.6 nMK2[34, 35]
M and M-like proteinStreptococcus canisAnchoredMini-plg: 𝐾 𝐷 = 2.7 nMHigh affinity for plg K5[28]
Streptococcus equiPlg: 𝐾 𝐷 = 18 nMPlg binding not competed out by excess K1–3, but inhibited by EACA, suggesting a role for K4 or K5[54]
Mhp 107Mycoplasma hyopneumoniae AnchoredPlg (porcine): 𝐾 𝐷 = NDND[26]
MPL36Leptospira interrogansAnchoredND[52]
Outer surface protein A (OspA)Borrelia burgdorferiAnchoredGlu-plg: 𝐾 𝐷 = 260 μMInteracts with LBS within plg and pln. Bound plg can be activated by both uPA and tPA[55]
70 kDa surface protein (OppA)Borrelia burgdoferiAnchoredNDND[55, 56]
PavBStreptococcus pneumoniaAnchoredNDND[57]
PfbBStreptococcus pneumoniaAnchoredNDND[58]
PfbAStreptococcus pneumoniaAnchoredNDND[59]
Plasminogen-binding protein (Pbp)Bacteroides fragilisAnchoredNDND[60]
PbbA and pgbBHelicobacter pyloriAnchoredNDInteracts with LBS of plg[61]
P116Mycoplasma hyopneumoniae AnchoredAsp-plg (porcine): 𝐾 𝐷 = 44 nMND[26]
Protein EHaemophilus influenzaeAnchoredNDInteracts with LBS of plg[62]
Type 1fimbriaeEscherichia coliAnchoredGlu-plg: 𝐾 𝐷 = 200 nMND[63, 64]
Streptococcus pneumoniaePlg: 𝐾 𝐷 1 = 0.55 nM; 𝐾 𝐷 2 = 86.2 nMResidues 248–256; C-terminal lysyl residues LL433 and LL434. Interacts with LBS within Plg[6567]
Streptococcus pyogenesGlu-Plg: 𝐾 𝐷 = 1.6 nM; Lys-plg: 𝐾 𝐷 = 127 nMC-terminal lysine residues K434 and K434; Residues 252–255. Interacts with LBS within Plg[68, 69]
Streptococcus suisPlg: 𝐾 𝐷 = 14 nMContains internal nonapeptide motif[70]
Bifidobacterium lactisPlg: 𝐾 𝐷 = 42 nMLysine and glutamic acid residues K251, K251, and E252[30]
Bacillus anthracosisNDPlg binding partially mediated by C-terminal lysine. Interacts with LBS within Plg[71, 72]
α-enolaseNeisseria meningitidisNonanchoredNDUndefined internal plg-binding motif[73]
Streptococcus mutansNDBinds plg via C-terminal lysine[74]
Streptococcus agalactiaeGlu-Plg: ND; Lys-Plg: NDND[75]
Mycoplasma gallisepticumNDND[27]
Mycoplasma fermentasNDND[76]
Borrelia burgdorferiGlu-plg: 𝐾 𝐷 = 125 nMInteracts with LBS within Plg[77]
Ag85BMycobacterium tuberculosisNonanchoredNDInteracts with LBS within plg[49]
AspartaseHaemophilus influenzaeNonanchoredNDK4. Potent stimulator of tPA but not uPA[78]
Bifidobacterium animalisPlg: 𝐾 𝐷 = 11.97 nMInteracts with LBS within plg[79]
DNaKNeisseria meningitidisNonanchoredNDUndefined internal plg-binding motif[73]
Mycobacterium tuberculosisNDInteracts with LBS within plg[49]
Elongation factor-tu (EF-tu)Bacillus anthracosisNonanchoredNDInteracts with LBS within plg[71]
Fructose-1,6-bisphosphate aldolaseMycoplasma tuberculosisNonanchoredPlg: 𝐾 𝐷 = 6.73 nMND [80]
Streptococcus pneumoniaePln: 𝐾 𝐷 1 = 28 nM; 𝐾 𝐷 2 = 52 nM
Plg: 𝐾 𝐷 1 = 0.43 μM; 𝐾 𝐷 2 = 0.16 nM
Binds plg via two C-terminal lysine residues separated by isoleucine and alanine[67, 81]
Glyceraldehyde 3-phphate dehydrogenase (GAPDH; GAPC; SDH; Plr)Streptococcus pyogenesNonanchoredNDND[82]
Bacillus anthracis Plg: 𝐾 𝐷 = 78.5 nM; 572 nMND[83]
Streptococcus equisimilisPlg: 𝐾 𝐷 = 220 nM; Pln: 𝐾 𝐷 = 25 nMND[84]
PeroxiredoxinNeisseria meningitidisNonanchoredNDUndefined internal plg-binding motif[73]
Phosphoglycerate kinaseStreptococcus equisimilisNonanchoredNDShown to bind both plg and pln[85]
SkzLStreptococcus agalactiaeNonanchoredGlu-plg: 𝐾 𝐷 = 3−16 nM; Lys-plg: 𝐾 𝐷 = 80 nM; Pln 𝐾 𝐷 = 50 nMND[86]

ND: not determined, plg: plasminogen, pln: plasmin, LBS: lysine binding site, K1–5: kringle 1–5.