Vimentin Is an Attachment Receptor for Mycoplasma pneumoniae P1 Protein

Peng, Ke; Liao, Yating; Li, Xia; Zeng, Dongdong; Ye, Youyuan; Chen, Li; Zeng, Zhuo; Zeng, Yanhua

doi:10.1128/spectrum.04489-22

Cited by 2 publications

(3 citation statements)

References 57 publications

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“…The ability of rLP78 to bind cell membrane proteins were determined by a microtiter plate adhesion assay (MPAA) and western blotting as previously described ( Li et al, 2022 ; Peng, et al, 2023 ). For MPAA, membrane and cytoplasmic proteins were extracted from 2 × 10 7 DF-1 cells using a commercial kit (Beyotime, China) according to the manufacturer’s instructions.…”

Section: Methodsmentioning

confidence: 99%

Mycoplasma synoviae LP78 is a fibronectin/plasminogen binding protein, putative adhesion, and potential diagnostic antigen

Han,

Wang,

Wang

et al. 2024

Front. Microbiol.

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Mycoplasma synoviae (M. synoviae) is one of the major poultry pathogens causing infectious synovitis, airsacculitis, a high incidence of shell breakage, and egg production loss. However, the pathogenesis of M. synoviae remains unclear. Adhesion of mycoplasmas to host cells is a crucial step in infection and colonization. The purpose of this study was to determine the adhesive function of a putative P80 family lipoprotein (LP78) and evaluate its application in the detection of antibodies against M. synoviae. Recombinant LP78 (rLP78) was expressed in the supernatant component of Escherichia coli and mouse anti-rLP78 serum was prepared. Bioinformatic analysis and western blotting results revealed that LP78 was conservative among M. synoviae strains. It was distributed not only in the cytoplasm but also on the membrane of M. synoviae through western blotting and indirect immunofluorescence (IFA). The adherence of M. synoviae to DF-1 cells was significantly inhibited by mouse anti-rLP78 serum (p < 0.01). IFA revealed that rLP78 adhered to DF-1 cells, and this adherence was prevented by mouse anti-rLP78 serum. Furthermore, rLP78 was found to bind to the DF-1 cells membrane proteins in a dose-dependent manner by enzyme-linked immunosorbent assay (ELISA). Screening of DF-1 cells membrane proteins by western blotting showed that proteins with molecular weight of 35–40 kDa and 55–70 kDa bound to rLP78. Moreover, rLP78 was identified to be a fibronectin/plasminogen binding protein. The sensitivity and specificity of rLP78-based iELISA were 85.7 and 94.1%, respectively. The maximum dilution of positive serum (HI titer, 1:128) detected via rLP78-based iELISA was 1:6,400, whereas that detected using a commercial ELISA kit was 1:12,800–1:25,600. Both rLP78-based iELISA and the commercial ELISA kit detected seroconversion after 7 days of challenge and immunization. No cross-reactivity with positive sera against other avian pathogens was observed in rLP78-based iELISA. Collectively, these results indicate that LP78 is a fibronectin/plasminogen-binding adhesion protein of M. synoviae and a potential diagnostic antigen. The present study will facilitate a better understanding of the pathogenesis of M. synoviae and the development of new diagnostic.

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Section: Methodsmentioning

confidence: 99%

Mycoplasma synoviae LP78 is a fibronectin/plasminogen binding protein, putative adhesion, and potential diagnostic antigen

Han,

Wang,

Wang

et al. 2024

Front. Microbiol.

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“…84 The P1 protein, a major immunogenic protein of Mycoplasma pneumoniae, was found to interact with vimentin and facilitate adhesion to bronchial epithelial cells. 85 Interaction of internalin (InlF) of Listeria monocytogenes and surfacelocalized vimentin was found to be responsible for bloodbrain barrier crossing and, subsequently, invasion into the brain. 86 Mycobacterium tuberculosis-infected monocytes had upregulated expression of cell surface vimentin on macrophages that enhanced the lysis of infected monocytes by natural killer cells.…”

Section: Role Of Extracellular Vimentin In Host-pathogen Interactionsmentioning

confidence: 99%

“…Similarly, Escherichia coli K1 relies on the interaction between cell surface vimentin and the bacterial virulence factor IbeA to invade brain endothelial cells 84 . The P1 protein, a major immunogenic protein of Mycoplasma pneumoniae , was found to interact with vimentin and facilitate adhesion to bronchial epithelial cells 85 . Interaction of internalin (InlF) of Listeria monocytogenes and surface‐localized vimentin was found to be responsible for blood–brain barrier crossing and, subsequently, invasion into the brain 86 .…”

Section: Role Of Extracellular Vimentin In Host–pathogen Interactionsmentioning

confidence: 99%

Extracellular vimentin as a modulator of the immune response and an important player during infectious diseases

Suprewicz,

Zakrzewska,

Okła

et al. 2024

Immunol Cell Biol

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Vimentin, an intermediate filament protein primarily recognized for its intracellular role in maintaining cellular structure, has recently garnered increased attention and emerged as a pivotal extracellular player in immune regulation and host–pathogen interactions. While the functions of extracellular vimentin were initially overshadowed by its cytoskeletal role, accumulating evidence now highlights its significance in diverse physiological and pathological events. This review explores the multifaceted role of extracellular vimentin in modulating immune responses and orchestrating interactions between host cells and pathogens. It delves into the mechanisms underlying vimentin's release into the extracellular milieu, elucidating its unconventional secretion pathways and identifying critical molecular triggers. In addition, the future perspectives of using extracellular vimentin in diagnostics and as a target protein in the treatment of diseases are discussed.

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Vimentin Is an Attachment Receptor for Mycoplasma pneumoniae P1 Protein

Cited by 2 publications

References 57 publications

Mycoplasma synoviae LP78 is a fibronectin/plasminogen binding protein, putative adhesion, and potential diagnostic antigen

Mycoplasma synoviae LP78 is a fibronectin/plasminogen binding protein, putative adhesion, and potential diagnostic antigen

Extracellular vimentin as a modulator of the immune response and an important player during infectious diseases

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