Abstract

Here, we provide the dataset associated with our research article on comprehensive screening of Brucella immunoreactive proteins using sera of naturally infected hosts published in Biochemical and Biophysical Research Communications Wareth et al., 2015 [1]. Whole-cell protein extracts were prepared from Brucella abortus and Brucella melitensis, separated using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and subsequently western blotting was carried out using sera from bovines (cows and buffaloes) and small ruminants (goats and sheep). The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium (http://proteomecentral.proteomexchange.org) via the PRIDE partner repository [2] with the dataset identifiers PXD001270 and DOI:10.6019/PXD001270.

Highlights

  • Mass spectrometry data from proteomics-based screening of immunoreactive proteins of fully virulent Brucella strains using sera from naturally infected animals

  • The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium via the PRIDE partner repository [2] with the dataset identifiers PXD001270 and DOI:10.6019/PXD001270. & 2015 The Authors

  • Experimental factors a) Fully virulent Brucella strains: B. abortus isolated from an infected cow in Turkey and B. melitensis isolated from an infected sheep in China

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Summary

Data Article

Gamal Wareth a,b, Falk Melzer b, Christoph Weise c, Heinrich Neubauer b, Uwe Roesler a, Jayaseelan Murugaiyan a,n a Institute of Animal Hygiene and Environmental Health, Centre for Infectious Medicine, Freie Universität Berlin, Berlin, Germany b Friedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Institute of Bacterial Infections and Zoonoses, Jena, Germany c Institute for Chemistry and Biochemistry, Freie Universität Berlin, Berlin, Germany article info. We provide the dataset associated with our research article on comprehensive screening of Brucella immunoreactive proteins using sera of naturally infected hosts published in Biochemical and Biophysical Research Communications Wareth et al, 2015 [1]. The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium (http://proteomecentral.proteomexchange.org) via the PRIDE partner repository [2] with the dataset identifiers PXD001270 and DOI:10.6019/PXD001270.

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