Background Mycoplasmas are the simplest bacteria capable of autonomous replication. Their evolution proceeded from gram-positive bacteria, with the loss of many biosynthetic pathways and of the cell wall. In this work, the liposoluble protein complement ofMycoplasma agalactiae, a minimal bacterial pathogen causing mastitis, polyarthritis, keratoconjunctivitis, and abortion in small ruminants, was subjected to systematic characterization in order to gain insights into its membrane proteome composition. Results The selective enrichment forM. agalactiaePG2T liposoluble proteins was accomplished by means of Triton X-114 fractionation. Liposoluble proteins were subjected to 2-D PAGE-MS, leading to the identification of 40 unique proteins and to the generation of a reference 2D map of theM. agalactiaeliposoluble proteome. Liposoluble proteins from the type strain PG2 and two field isolates were then compared by means of 2D DIGE, revealing reproducible differences in protein expression among isolates. An in-depth analysis was then performed by GeLC-MS/MS in order to achieve a higher coverage of the liposoluble proteome. Using this approach, a total of 194 unique proteins were identified, corresponding to 26% of allM. agalactiaePG2T genes. A gene ontology analysis and classification for localization and function was also carried out on all protein identifications. Interestingly, the 11.5% of expressed membrane proteins derived from putative horizontal gene transfer events. Conclusions This study led to the in-depth systematic characterization of theM. agalactiaeliposoluble protein component, providing useful insights into its membrane organization.

The Liposoluble proteome ofMycoplasma agalactiae: an insight into the minimal protein complement of a bacterial membrane / Chessa, Bernardo; Uzzau, Sergio; Alberti, Alberto; Pittau, Marco; Cacciotto, Carla; Addis, Maria Filippa; Coradduzza, Elisabetta; Carcangiu, Laura; Pagnozzi, Daniela. - 10:(2010), pp. 225-236. [10.1186/1471-2180-10-225]

The Liposoluble proteome ofMycoplasma agalactiae: an insight into the minimal protein complement of a bacterial membrane

Chessa, Bernardo;Uzzau, Sergio;Alberti, Alberto;Pittau, Marco;Addis, Maria Filippa;Coradduzza, Elisabetta;
2010

Abstract

Background Mycoplasmas are the simplest bacteria capable of autonomous replication. Their evolution proceeded from gram-positive bacteria, with the loss of many biosynthetic pathways and of the cell wall. In this work, the liposoluble protein complement ofMycoplasma agalactiae, a minimal bacterial pathogen causing mastitis, polyarthritis, keratoconjunctivitis, and abortion in small ruminants, was subjected to systematic characterization in order to gain insights into its membrane proteome composition. Results The selective enrichment forM. agalactiaePG2T liposoluble proteins was accomplished by means of Triton X-114 fractionation. Liposoluble proteins were subjected to 2-D PAGE-MS, leading to the identification of 40 unique proteins and to the generation of a reference 2D map of theM. agalactiaeliposoluble proteome. Liposoluble proteins from the type strain PG2 and two field isolates were then compared by means of 2D DIGE, revealing reproducible differences in protein expression among isolates. An in-depth analysis was then performed by GeLC-MS/MS in order to achieve a higher coverage of the liposoluble proteome. Using this approach, a total of 194 unique proteins were identified, corresponding to 26% of allM. agalactiaePG2T genes. A gene ontology analysis and classification for localization and function was also carried out on all protein identifications. Interestingly, the 11.5% of expressed membrane proteins derived from putative horizontal gene transfer events. Conclusions This study led to the in-depth systematic characterization of theM. agalactiaeliposoluble protein component, providing useful insights into its membrane organization.
The Liposoluble proteome ofMycoplasma agalactiae: an insight into the minimal protein complement of a bacterial membrane / Chessa, Bernardo; Uzzau, Sergio; Alberti, Alberto; Pittau, Marco; Cacciotto, Carla; Addis, Maria Filippa; Coradduzza, Elisabetta; Carcangiu, Laura; Pagnozzi, Daniela. - 10:(2010), pp. 225-236. [10.1186/1471-2180-10-225]
File in questo prodotto:
File Dimensione Formato  
Cacciotto_C_Liposoluble_proteome_of_Mycoplasma.pdf

accesso aperto

Tipologia: Versione editoriale (versione finale pubblicata)
Licenza: Creative commons
Dimensione 3.42 MB
Formato Adobe PDF
3.42 MB Adobe PDF Visualizza/Apri

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11388/264839
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus ND
  • ???jsp.display-item.citation.isi??? ND
social impact