Major Outer Membrane Protein B (MopB)

Major Outer Membrane Protein B (MopB) is a highly abundant and conserved surface-exposed protein found in several Gram-negative bacteria, most notably the plant pathogen Xylella fastidiosa and the human opportunistic pathogen Stenotrophomonas maltophilia [6, 59]. It belongs to the OmpA family of porins and is essential for maintaining the structural integrity of the bacterial outer membrane [26, 31]. MopB plays a pleiotropic role in bacterial virulence, being required for biofilm formation, cell-to-cell aggregation, and type IV pilus-mediated twitching motility [21, 22]. In some bacterial species, MopB is also an alias for the chaperonin GroEL, which is involved in protein folding and stress response [57, 63]. Due to its high abundance and accessibility on the cell surface, MopB has been identified as a significant therapeutic target [26, 48]. In agricultural biotechnology, engineered protein chimeras (such as HNE-cecropin B) have been developed to recognize and cleave MopB, leading to pathogen lysis and protection against diseases like Pierce's disease in grapevines [26, 47]. In clinical research, MopB is being explored as a potential vaccine candidate and a target for recombinant antibodies to treat multidrug-resistant bacterial infections [31, 55, 62].

Other names

OmpA-like proteinPD1709SmMopBGroELChaperonin 60Myelin-associated oligodendrocytic basic proteinMOBPMolybdenum-binding protein B

The HNE-cecropin B chimera targets MopB through its elastase domain, which recognizes and cleaves the protein, while the cecropin B domain creates pores in the bacterial membrane to induce lysis. Anti-MopB antibodies function by agglutinating bacteria and blocking their attachment to host surfaces or vectors.