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Predominant Single Stable VpmaV Expression in Strain GM139 and Major Differences with Type Strain PG2

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Journal Animals (Basel)
Date 2022 Feb 15
PMID 35158589
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Abstract

Although mycoplasmas have a reduced genome and no cell wall, they have important mechanisms for the antigenic variation in surface lipoproteins that modulate their interactions with the host. , the main etiological agent of contagious agalactia, has a multigene family involved in the high-frequency phase variation in surface lipoproteins called variable proteins of (Vpmas). The Vpma lipoproteins are involved in the immune evasion, colonization, dissemination, and persistence of in the host. In this paper, we evaluate the Vpma phenotypic profiles of two different strains of namely, GM139 and the type strain PG2, to assess possible correlations between Vpma phase variability and the geographic localization, animal origin, and pathogenicity of these two strains. Using monospecific Vpma antibodies against individual Vpmas in immunoblots, we demonstrate that, unlike PG2, which expresses six Vpma proteins with high-frequency phase variation, colonies of GM139 predominantly express VpmaV and do not exhibit any sectoring phenotype for any Vpma. Since VpmaV is one of the most important Vpmas for cell adhesion and invasion, its predominant sole expression in GM139 without high-frequency variation may be the basis of the differential pathogenicity of GM139 and PG2. Additionally, MALDI-ToF MS analysis also demonstrates significant differences between these two strains and their relatedness with other strains.

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References
1.
Bergonier D, Berthelot X, Poumarat F . Contagious agalactia of small ruminants: current knowledge concerning epidemiology, diagnosis and control. Rev Sci Tech. 1998; 16(3):848-73. DOI: 10.20506/rst.16.3.1062. View

2.
Kumar A, Rahal A, Chakraborty S, Verma A, Dhama K . Mycoplasma agalactiae, an Etiological Agent of Contagious Agalactia in Small Ruminants: A Review. Vet Med Int. 2014; 2014:286752. PMC: 4109668. DOI: 10.1155/2014/286752. View

3.
Nouvel L, Sirand-Pugnet P, Marenda M, Sagne E, Barbe V, Mangenot S . Comparative genomic and proteomic analyses of two Mycoplasma agalactiae strains: clues to the macro- and micro-events that are shaping mycoplasma diversity. BMC Genomics. 2010; 11:86. PMC: 2824730. DOI: 10.1186/1471-2164-11-86. View

4.
Chopra-Dewasthaly R, Zimmermann M, Rosengarten R, Citti C . First steps towards the genetic manipulation of Mycoplasma agalactiae and Mycoplasma bovis using the transposon Tn4001mod. Int J Med Microbiol. 2005; 294(7):447-53. PMC: 4509485. DOI: 10.1016/j.ijmm.2004.09.010. View

5.
Bergonier D, De Simone F, Russo P, Solsona M, Lambert M, Poumarat F . Variable expression and geographic distribution of Mycoplasma agalactiae surface epitopes demonstrated with monoclonal antibodies. FEMS Microbiol Lett. 1996; 143(2-3):159-65. DOI: 10.1111/j.1574-6968.1996.tb08475.x. View