Skip to main content
SpringerLink
Log in

Identification of Mycoplasma suis MSG1 interaction proteins on porcine erythrocytes

  • Original Paper
  • Published:
Archives of Microbiology Aims and scope Submit manuscript

Abstract

Adhesion protein MSG1 mediating adherence to porcine erythrocytes in Mycoplasma suis (M. suis) invasion has been identified previously. In order to determine the host membrane proteins that interact with MSG1, recombinant His-tagged MSG1 (rMSG1) was used to screen for interacting proteins in the protein extracts of porcine erythrocyte membrane. Potential rMSG1-interacting proteins were initially identified as band 3 and β-actin with molecular weight of 46 and 45 kDa, respectively. Immune fluorescence results showed that rMSG1 can specifically bind with the β-actin of HeLa, BHK-21, and HEK-293A cells, respectively. RNA interference assays further demonstrated that the interaction between β-actin and rMSG1 on HeLa cells was specific and dose dependent. Confocal microscopy showed that both rMSG1 and M. suis can partially co-localize with β-actin on the surface of porcine erythrocytes. Pull-down assays showed that rMSG1 can directly interact with β-actin. Our study is the first to report the interaction of MSG1 with β-actin, which will be of help to understand the pathogenesis of M. suis and develop a cultivation system.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5

Similar content being viewed by others

References

  • Alvarez RABM, Baseman JB (2003) Surface localized glyceraldehydes-3-phosphate dehydrogenase of Mycoplasma genitalium binds mucin. Mol Microbiol 48:1417–1425

    Article  CAS  PubMed  Google Scholar 

  • Felder KMHK, Heinritzi K, Ritzmann M, Hoelzle LE (2010) Antibodies to actin in autoimmune haemolytic anaemia. BMC Vet Res 6:18

    Article  PubMed Central  PubMed  Google Scholar 

  • Gresham ARJ, Tribe H, Phipps LP (1994) Eperythrozoon suis in weaned pigs. Vet Rec 134:71–72

    Article  CAS  PubMed  Google Scholar 

  • Heinritzi K (1989) Eperythrozoon infection in swine as a disease factor. Berl Munch Tierarztl Wochenschr 102:337–342

    Google Scholar 

  • Henderson JPOHJ, Hawe SM, Pratt MC (1997) Anaemia and low viability in piglets infected with Eperythrozoon suis. Vet Rec 140:144–146

    Article  CAS  PubMed  Google Scholar 

  • Hoelzle LE, Hoelzle K, Ritzmann M, Heinritzi K, Wittenbrink MM (2006) Mycoplasma suis antigens recognized during humoral immune response in experimentally infected pigs. Clin Vaccine Immunol 13:116–122. doi:10.1128/CVI.13.1.116-122.2006

    Article  PubMed Central  CAS  PubMed  Google Scholar 

  • Hoelzle LE et al (2007) First identification and functional characterization of an immunogenic protein in unculturable haemotrophic Mycoplasmas (Mycoplasma suis HspA1). FEMS Immunol Med Microbiol 49:215–223. doi:10.1111/j.1574-695X.2006.00184.x

    Article  CAS  PubMed  Google Scholar 

  • Jin HAS, Aqarwal S, Pancholi V (2011) Surface export of GAPDH/SDH, a glycolytic enzyme, is essential for streptococcus pyogenes virulence. MBio 2:e00068-00011

    Article  Google Scholar 

  • Le H (2008) Haemotrophic mycoplasmas: recent advances in Mycoplasma suis. Vet Microbiol 130:215–226

    Article  Google Scholar 

  • LE Hoelzle AD, Hoelzle K, Heinritzi K, Wittenbrink MM (2003) Development of a diagnostic PCR assay based on novel DNA sequences for the detection of Mycoplasma suis (Eperythrozoon suis) in porcine blood. Vet Microbiol 93:185–196

    Article  CAS  PubMed  Google Scholar 

  • LE Hoelzle HK, Helbling M, Aupperle H, Schoon Heinz et al (2007) MSG1, a surface-localised protein of Mycoplasma suis is involved in the adhesion to erythrocytes. Microbes Infect 9:466–474

    Article  CAS  PubMed  Google Scholar 

  • Messick JB (2004) Hemotrophic mycoplasmas (haemoplasmas): a review and new insights into pathogenic potential. Vet Clin Pathol 33:2–13

    Article  PubMed  Google Scholar 

  • Pancholi VFV (1992) A major surface protein on group A streptococci is a glyceraldehydes-3-phosphate dehydrogenase with multiple binding activity. J Exp Med 176:415–426

    Article  CAS  PubMed  Google Scholar 

  • Pospischil AHR (1982) Eperythrozoon suis in naturally infected pigs: a light and electron microscopic study. Vet Pathol 19:651–657

    Article  CAS  PubMed  Google Scholar 

  • Reyes-del Valle J, del Angel RM (2004) Isolation of putative dengue virus receptor molecules by affinity chromatography using a recombinant E protein ligand. J Virol Methods 116:95–102

    Article  CAS  PubMed  Google Scholar 

  • Seifert KNMW, Bleiweis AS, Brady LJ (2003) Characterization of group B streptococcal glyceraldehyde-3-phosphate dehydrogenase: surface localization, enzymatic activity, and protein-protein interactions. Can J Microbiol 49:350–356

    Article  CAS  PubMed  Google Scholar 

  • Strait EL, Hawkins PA, Wilson WD (2012) Dysgalactia associated with Mycoplasma suis infection in a sow herd. J Am Vet Med Assoc 241:1666–1667. doi:10.2460/javma.241.12.1666

    Article  PubMed  Google Scholar 

  • Zachary JFBE (1985a) Erythrocyte membrane alterations associated with the attachment and replication of Eperythrozoon suis: a light and electron microscopic study. Vet Pathol 22:164–170

    Article  CAS  PubMed  Google Scholar 

  • Zachary JFSA (1985b) Experimental porcine eperythrozoonosis: T-lymphocyte suppression and misdirected immune responses. Am J Vet Res 46:821–830

    CAS  PubMed  Google Scholar 

  • Zhang CY, Li YF, Jiang P, Chen W (2012) Use of MSG1 protein in a novel blocking ELISA for the detection of Mycoplasma suis infection. Vet J 193:535–538. doi:10.1016/j.tvjl.2011.12.017

    Article  CAS  PubMed  Google Scholar 

Download references

Acknowledgments

This research was supported by public welfare Grants from the Ministry of Agriculture, The People’s Republic of China (200903036-10), and Priority Academic Program Development of Jiangsu Higher Education Institutions (PAPD).

Conflict of interest

Authors have no competing interest to declare.

Author information

Authors and Affiliations

  1. Key Laboratory of Bacteriology, Ministry of Agriculture, College of Veterinary Medicine, Nanjing Agricultural University, 210095, Nanjing, China

    Yaning Zhang, Yao Zou, Peipei Ma, Yufeng Li & Ping Jiang

  2. Department of Epidemiology and Public Health, Faculty of Veterinary Science, University of Veterinary and Animal Sciences, Lahore, Pakistan

    Hassan Mushtaq Muhammad

Authors
  1. Yaning Zhang
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Yao Zou
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Peipei Ma
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Hassan Mushtaq Muhammad
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Yufeng Li
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. Ping Jiang
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Yufeng Li.

Additional information

Communicated by Erko Stackebrandt.

Yaning Zhang and Yao Zou are the coauthors.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Zhang, Y., Zou, Y., Ma, P. et al. Identification of Mycoplasma suis MSG1 interaction proteins on porcine erythrocytes. Arch Microbiol 197, 277–283 (2015). https://doi.org/10.1007/s00203-014-1050-7

Download citation

  • Received:

  • Revised:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s00203-014-1050-7

Keywords

Search

Navigation