Hydrogen peroxide and hypochlorous acid influx through the major S. Typhimurium porin OmpD is affected by substitution of key residues of the channel

Daniel Aguayo; Nicolás Pacheco; Eduardo H. Morales; Bernardo Collao; Roberto Luraschi; Carolina Cabezas; Paulina Calderón; Fernando González-Nilo; Fernando Gil; Iván L. Calderón; Claudia P. Saavedra

doi:10.1016/j.abb.2015.01.005

Hydrogen peroxide and hypochlorous acid influx through the major S. Typhimurium porin OmpD is affected by substitution of key residues of the channel

Daniel Aguayo, Nicolás Pacheco, Eduardo H. Morales, Bernardo Collao, Roberto Luraschi, Carolina Cabezas, Paulina Calderón, Fernando González-Nilo, Fernando Gil, Iván L. Calderón, Claudia P. Saavedra

Life Sciences School

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

15 Citations (Scopus)

Abstract

OmpD is the major Salmonella enterica serovar Typhimurium (S. Typhimurium) porin and mediates hydrogen peroxide (H₂O₂) influx. The results described herein extend this finding to hypochlorous acid (HOCl), another reactive oxygen species that is also part of the oxidative burst generated by the phagosome. S. Typhimurium cells lacking OmpD show decreased HOCl influx, and OmpD-reconstituted proteoliposomes show an increase in the uptake of the toxic compound. To understand this physiologically relevant process, we investigated the role of key OmpD residues in H₂O₂ and NaOCl transport. Using a theoretical approach, residue K16 was defined as a major contributor to the channel electrostatic properties, and E111 was shown to directly participate in the size-exclusion limit of the channel. Together, we provide theoretical, genetic, and biochemical evidence that OmpD mediates H₂O₂ and NaOCl uptake, and that key residues of the channel are implicated in this process.

Original language	English
Pages (from-to)	38-45
Number of pages	8
Journal	Archives of Biochemistry and Biophysics
Volume	568
DOIs	https://doi.org/10.1016/j.abb.2015.01.005
Publication status	Published - 15 Feb 2015

Keywords

Homology modeling
Hydrogen peroxide
Hypochlorous acid
Molecular simulations
OmpD porin

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology

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10.1016/j.abb.2015.01.005

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Aguayo, D., Pacheco, N., Morales, E. H., Collao, B., Luraschi, R., Cabezas, C., Calderón, P., González-Nilo, F., Gil, F., Calderón, I. L., & Saavedra, C. P. (2015). Hydrogen peroxide and hypochlorous acid influx through the major S. Typhimurium porin OmpD is affected by substitution of key residues of the channel. Archives of Biochemistry and Biophysics, 568, 38-45. https://doi.org/10.1016/j.abb.2015.01.005

@article{232f5820baef49578307178e6acaefa4,

title = "Hydrogen peroxide and hypochlorous acid influx through the major S. Typhimurium porin OmpD is affected by substitution of key residues of the channel",

abstract = "OmpD is the major Salmonella enterica serovar Typhimurium (S. Typhimurium) porin and mediates hydrogen peroxide (H2O2) influx. The results described herein extend this finding to hypochlorous acid (HOCl), another reactive oxygen species that is also part of the oxidative burst generated by the phagosome. S. Typhimurium cells lacking OmpD show decreased HOCl influx, and OmpD-reconstituted proteoliposomes show an increase in the uptake of the toxic compound. To understand this physiologically relevant process, we investigated the role of key OmpD residues in H2O2 and NaOCl transport. Using a theoretical approach, residue K16 was defined as a major contributor to the channel electrostatic properties, and E111 was shown to directly participate in the size-exclusion limit of the channel. Together, we provide theoretical, genetic, and biochemical evidence that OmpD mediates H2O2 and NaOCl uptake, and that key residues of the channel are implicated in this process.",

keywords = "Homology modeling, Hydrogen peroxide, Hypochlorous acid, Molecular simulations, OmpD porin",

author = "Daniel Aguayo and Nicol{\'a}s Pacheco and Morales, {Eduardo H.} and Bernardo Collao and Roberto Luraschi and Carolina Cabezas and Paulina Calder{\'o}n and Fernando Gonz{\'a}lez-Nilo and Fernando Gil and Calder{\'o}n, {Iv{\'a}n L.} and Saavedra, {Claudia P.}",

note = "Funding Information: This work was supported in part by FONDECYT grants CS #1120384 and DA #11130576 and Millenium Initiative 09-022-F (FGN). ",

year = "2015",

month = feb,

day = "15",

doi = "10.1016/j.abb.2015.01.005",

language = "English",

volume = "568",

pages = "38--45",

journal = "Archives of Biochemistry and Biophysics",

issn = "0003-9861",

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Aguayo, D, Pacheco, N, Morales, EH, Collao, B, Luraschi, R, Cabezas, C, Calderón, P, González-Nilo, F , Gil, F , Calderón, IL & Saavedra, CP 2015, 'Hydrogen peroxide and hypochlorous acid influx through the major S. Typhimurium porin OmpD is affected by substitution of key residues of the channel', Archives of Biochemistry and Biophysics, vol. 568, pp. 38-45. https://doi.org/10.1016/j.abb.2015.01.005

TY - JOUR

T1 - Hydrogen peroxide and hypochlorous acid influx through the major S. Typhimurium porin OmpD is affected by substitution of key residues of the channel

AU - Aguayo, Daniel

AU - Pacheco, Nicolás

AU - Morales, Eduardo H.

AU - Collao, Bernardo

AU - Luraschi, Roberto

AU - Cabezas, Carolina

AU - Calderón, Paulina

AU - González-Nilo, Fernando

AU - Gil, Fernando

AU - Calderón, Iván L.

AU - Saavedra, Claudia P.

N1 - Funding Information: This work was supported in part by FONDECYT grants CS #1120384 and DA #11130576 and Millenium Initiative 09-022-F (FGN).

PY - 2015/2/15

Y1 - 2015/2/15

N2 - OmpD is the major Salmonella enterica serovar Typhimurium (S. Typhimurium) porin and mediates hydrogen peroxide (H2O2) influx. The results described herein extend this finding to hypochlorous acid (HOCl), another reactive oxygen species that is also part of the oxidative burst generated by the phagosome. S. Typhimurium cells lacking OmpD show decreased HOCl influx, and OmpD-reconstituted proteoliposomes show an increase in the uptake of the toxic compound. To understand this physiologically relevant process, we investigated the role of key OmpD residues in H2O2 and NaOCl transport. Using a theoretical approach, residue K16 was defined as a major contributor to the channel electrostatic properties, and E111 was shown to directly participate in the size-exclusion limit of the channel. Together, we provide theoretical, genetic, and biochemical evidence that OmpD mediates H2O2 and NaOCl uptake, and that key residues of the channel are implicated in this process.

AB - OmpD is the major Salmonella enterica serovar Typhimurium (S. Typhimurium) porin and mediates hydrogen peroxide (H2O2) influx. The results described herein extend this finding to hypochlorous acid (HOCl), another reactive oxygen species that is also part of the oxidative burst generated by the phagosome. S. Typhimurium cells lacking OmpD show decreased HOCl influx, and OmpD-reconstituted proteoliposomes show an increase in the uptake of the toxic compound. To understand this physiologically relevant process, we investigated the role of key OmpD residues in H2O2 and NaOCl transport. Using a theoretical approach, residue K16 was defined as a major contributor to the channel electrostatic properties, and E111 was shown to directly participate in the size-exclusion limit of the channel. Together, we provide theoretical, genetic, and biochemical evidence that OmpD mediates H2O2 and NaOCl uptake, and that key residues of the channel are implicated in this process.

KW - Homology modeling

KW - Hydrogen peroxide

KW - Hypochlorous acid

KW - Molecular simulations

KW - OmpD porin

UR - http://www.scopus.com/inward/record.url?scp=84922032643&partnerID=8YFLogxK

U2 - 10.1016/j.abb.2015.01.005

DO - 10.1016/j.abb.2015.01.005

M3 - Article

C2 - 25600570

AN - SCOPUS:84922032643

SN - 0003-9861

VL - 568

SP - 38

EP - 45

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

ER -

Hydrogen peroxide and hypochlorous acid influx through the major S. Typhimurium porin OmpD is affected by substitution of key residues of the channel

Abstract

Keywords

ASJC Scopus subject areas

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