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Low calcium response antigen V (LcrV), commonly known as the V-antigen, is a multifunctional protein essential for the virulence of Yersinia pestis, the causative agent of the plague [1, 2]. It serves as a critical component of the Type III secretion system (T3SS), specifically forming the needle tip complex that facilitates the translocation of effector proteins, known as Yersinia outer proteins (Yops), into host cells [3, 4]. Once inside, these Yops disrupt host cell signaling and suppress the immune response [7, 9]. LcrV also possesses independent immunomodulatory functions, such as interacting with host Toll-like receptor 2 (TLR2) to induce the production of anti-inflammatory cytokines like IL-10, which further aids bacterial evasion of the host's innate immunity [8, 9]. Because of its central role in pathogenesis and its ability to elicit a protective immune response, LcrV is a primary target for the development of recombinant vaccines, such as the rF1-V fusion protein [5, 7]. Additionally, monoclonal antibodies targeting LcrV are being explored as therapeutic agents to neutralize the T3SS and enhance bacterial opsonization and clearance [1, 6].
Neutralization of the Type III secretion system needle tip to prevent effector protein translocation and enhancement of opsonophagocytosis.
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