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Dataset of single nucleotide polymorphisms and comprehensive proteomic analysis of Streptococcus equi subsp. equi ATCC 39506.
Lee, Hayoung; Yun, Sung Ho; Hyon, Ju-Yong; Lee, Sang-Yeop; Yi, Yoon-Sun; Choi, Chi-Won; Jun, Sangmi; Park, Edmond Changkyun; Kim, Seung Il.
Afiliação
  • Lee H; Research Center for Bioconvergence Analysis, Korea Basic Science Institute (KBSI), Ochang 28119, Republic of Korea.
  • Yun SH; Center for Convergent Research of Emerging Virus Infection, Korea Research Institute of Chemical Technology (KRICT), Daejeon 34114, Republic of Korea.
  • Hyon JY; Department of Bio-Analytical Science, University of Science and Technology, Daejeon 34113, Republic of Korea.
  • Lee SY; Center for Research Equipment, Korea Basic Science Institute, Ochang 28119, Republic of Korea.
  • Yi YS; Research Center for Bioconvergence Analysis, Korea Basic Science Institute (KBSI), Ochang 28119, Republic of Korea.
  • Choi CW; Research Center for Bioconvergence Analysis, Korea Basic Science Institute (KBSI), Ochang 28119, Republic of Korea.
  • Jun S; Center for Convergent Research of Emerging Virus Infection, Korea Research Institute of Chemical Technology (KRICT), Daejeon 34114, Republic of Korea.
  • Park EC; Center for Research Equipment, Korea Basic Science Institute, Ochang 28119, Republic of Korea.
  • Kim SI; KBNP Technology Institute, KBNP, INC., Heungan-daero 415, Dongan-Gu, Anyang, Gyeonggi, Republic of Korea.
Data Brief ; 38: 107402, 2021 Oct.
Article em En | MEDLINE | ID: mdl-34621931
ABSTRACT
Streptococcus equi subspecies equi (S. equi) is an opportunistic pathogen and a major causative agent of equine strangles, a contagious respiratory infection in horses and other equines. In this study, we provide the dataset associated with our research publication "Streptococcus equi-derived extracellular vesicles as a vaccine candidate against Streptococcus equi infections" [1]. We describe the genomic differences between S. equi 4047 and S. equi ATCC 39506 and outline the comprehensive proteome information of various fractions, including the whole cell lysate, membrane proteome, secretory proteome, and extracellular vesicle proteome. In addition, we included a dataset of highly immunoreactive proteins identified through immunoprecipitation. The specifications table provides a detailed summary of the gene annotation and quantitative information obtained for each proteome. The proteomics data were analyzed using shotgun proteomics with LTQ Velos and Q Exactive mass spectrometry in the data-dependent acquisition mode. We have deposited the acquired data, including the mass spectrometry raw files and exported MASCOT search results, in the PRIDE public repository under the accession numbers PXD025152 and PXD025527.
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Texto completo: 1 Base de dados: MEDLINE Idioma: En Ano de publicação: 2021 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Idioma: En Ano de publicação: 2021 Tipo de documento: Article