Functional Dissection of the PE Domain Responsible for Translocation of PE_PGRS33 across the Mycobacterial Cell Wall

A. Cascioferro; M.H. Daleke; M. Ventura; V. Dona; G. Delogu; G. Palu; W. Bitter; R. Manganelli

doi:https://doi.org/10.1371/journal.pone.0027713

Functional Dissection of the PE Domain Responsible for Translocation of PE_PGRS33 across the Mycobacterial Cell Wall

A. Cascioferro, M.H. Daleke, M. Ventura, V. Dona, G. Delogu, G. Palu, W. Bitter, R. Manganelli

Medical Microbiology and Infection Prevention (VUmc)

Research output: Contribution to journal › Article › Academic › peer-review

45 Citations (Scopus)

Abstract

PE are peculiar exported mycobacterial proteins over-represented in pathogenic mycobacterial species. They are characterized by an N-terminal domain of about 110 amino acids (PE domain) which has been demonstrated to be responsible for their export and localization. In this paper, we characterize the PE domain of PE_PGRS33 (PE

Original language	English
Article number	e27713
Journal	PLOS ONE
Volume	6
Issue number	11
DOIs	https://doi.org/10.1371/journal.pone.0027713
Publication status	Published - 2011

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https://doi.org/10.1371/journal.pone.0027713

Cite this

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abstract = "PE are peculiar exported mycobacterial proteins over-represented in pathogenic mycobacterial species. They are characterized by an N-terminal domain of about 110 amino acids (PE domain) which has been demonstrated to be responsible for their export and localization. In this paper, we characterize the PE domain of PE_PGRS33 (PE",

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AU - Cascioferro, A.

AU - Daleke, M.H.

AU - Ventura, M.

AU - Dona, V.

AU - Delogu, G.

AU - Palu, G.

AU - Bitter, W.

AU - Manganelli, R.

PY - 2011

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AB - PE are peculiar exported mycobacterial proteins over-represented in pathogenic mycobacterial species. They are characterized by an N-terminal domain of about 110 amino acids (PE domain) which has been demonstrated to be responsible for their export and localization. In this paper, we characterize the PE domain of PE_PGRS33 (PE

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