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The surface-localised α-enolase of Mycoplasma suis is an adhesion protein


Schreiner, S A; Sokoli, A; Felder, K M; Wittenbrink, M M; Schwarzenbach, S; Guhl, B; Hoelzle, K; Hoelzle, L E (2012). The surface-localised α-enolase of Mycoplasma suis is an adhesion protein. Veterinary Microbiology, 156(1-2):88-95.

Abstract

Mycoplasma suis belongs to the haemotrophic mycoplasmas which colonise red blood cells of a wide range of vertebrates. Adhesion to red blood cells is the crucial step in the unique lifecycle of M. suis. Due to the lack of a cultivation system, identification of adhesion structures has been difficult. So far, only one adhesion protein, i.e. MSG1 was identified. In order to determine further adhesion molecules of M. suis, we screened genomic M. suis libraries and performed Southern blot hybridisation analyses of genomic M. suis DNA. The α-enolase of M. suis was identified and analysed genetically and functionally. The encoding gene has 1623bp in size. The deduced amino acid sequence showed an overall identity of 59.6-65.1% to α-enolases of other pathogenic mycoplasmas. The 540aa M. suis α-enolase displays a size extension of about 90aa in comparison to α-enolases of other mycoplasmas. Recombinant α-enolase expressed in Escherichia coli demonstrated immunogenicity in experimentally infected pigs. Immunoblot, confocal laser scanning microscopy and immune electron microscopy analysis using antibodies against recombinant α-enolase, indicate the membrane and surface localisation of native α-enolase in M. suis, though no typical signal sequences exist. Furthermore, we showed that recombinant α-enolase binds to porcine erythrocyte lysate in a dose-dependent manner. E. coli transformants which express α-enolase on their surface acquire the ability to adhere to porcine red blood cells. In conclusion, our observations indicate that α-enolase could be involved in the adhesion of M. suis to porcine red blood cells.

Mycoplasma suis belongs to the haemotrophic mycoplasmas which colonise red blood cells of a wide range of vertebrates. Adhesion to red blood cells is the crucial step in the unique lifecycle of M. suis. Due to the lack of a cultivation system, identification of adhesion structures has been difficult. So far, only one adhesion protein, i.e. MSG1 was identified. In order to determine further adhesion molecules of M. suis, we screened genomic M. suis libraries and performed Southern blot hybridisation analyses of genomic M. suis DNA. The α-enolase of M. suis was identified and analysed genetically and functionally. The encoding gene has 1623bp in size. The deduced amino acid sequence showed an overall identity of 59.6-65.1% to α-enolases of other pathogenic mycoplasmas. The 540aa M. suis α-enolase displays a size extension of about 90aa in comparison to α-enolases of other mycoplasmas. Recombinant α-enolase expressed in Escherichia coli demonstrated immunogenicity in experimentally infected pigs. Immunoblot, confocal laser scanning microscopy and immune electron microscopy analysis using antibodies against recombinant α-enolase, indicate the membrane and surface localisation of native α-enolase in M. suis, though no typical signal sequences exist. Furthermore, we showed that recombinant α-enolase binds to porcine erythrocyte lysate in a dose-dependent manner. E. coli transformants which express α-enolase on their surface acquire the ability to adhere to porcine red blood cells. In conclusion, our observations indicate that α-enolase could be involved in the adhesion of M. suis to porcine red blood cells.

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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Center for Microscopy and Image Analysis
05 Vetsuisse Faculty > Institute of Veterinary Bacteriology
Dewey Decimal Classification:570 Life sciences; biology
610 Medicine & health
Language:English
Date:2012
Deposited On:18 Mar 2012 18:27
Last Modified:05 Apr 2016 15:39
Publisher:Elsevier
ISSN:0378-1135
Publisher DOI:https://doi.org/10.1016/j.vetmic.2011.10.010
PubMed ID:22047714
Permanent URL: https://doi.org/10.5167/uzh-59844

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