Role of protein glycosylation in Candida parapsilosis cell wall integrity and host interaction

Luis A. Pérez-García, Katalin Csonka, Arturo Flores-Carreón, Eine Estrada-Mata, Erika Mellado-Mojica, Tibor Németh, Luz A. López-Ramírez, Renata Toth, Mercedes G. López, C. Vízler, Annamaria Marton, Adél Tóth, Joshua D. Nosanchuk, A. Gácser, Héctor M. Mora-Montes

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

Candida parapsilosis is an important, emerging opportunistic fungal pathogen. Highly mannosylated fungal cell wall proteins are initial contact points with host immune systems. In Candida albicans, Och1 is a Golgi α1,6-mannosyltransferase that plays a key role in the elaboration of the N-linked mannan outer chain. Here, we disrupted C. parapsilosis OCH1 to gain insights into the contribution of N-linked mannosylation to cell fitness and to interactions with immune cells. Loss of Och1 in C. parapsilosis resulted in cellular aggregation, failure of morphogenesis, enhanced susceptibility to cell wall perturbing agents and defects in wall composition. We removed the cell wall O-linked mannans by β-elimination, and assessed the relevance of mannans during interaction with human monocytes. Results indicated that O-linked mannans are important for IL-1β stimulation in a dectin-1 and TLR4-dependent pathway; whereas both, N- and O-linked mannans are equally important ligands for TNFα and IL-6 stimulation, but neither is involved in IL-10 production. Furthermore, mice infected with C. parapsilosis och1Δ null mutant cells had significantly lower fungal burdens compared to wild-type (WT)-challenged counterparts. Therefore, our data are the first to demonstrate that C. parapsilosis N- and O-linked mannans have different roles in host interactions than those reported for C. albicans.

Original languageEnglish
Article number306
JournalFrontiers in Microbiology
Volume7
Issue numberMAR
DOIs
Publication statusPublished - Mar 8 2016

Fingerprint

Mannans
Glycosylation
Candida
Cell Wall
Candida albicans
Mannosyltransferases
Null Lymphocytes
Interleukin-1
Morphogenesis
Interleukin-10
Monocytes
Immune System
Interleukin-6
Ligands
Proteins

Keywords

  • Candida parapsilosis
  • Cell wall
  • Host-fungus interplay
  • Mannosylation pathway
  • Mannosyltransferase
  • Virulence

ASJC Scopus subject areas

  • Microbiology
  • Microbiology (medical)

Cite this

Pérez-García, L. A., Csonka, K., Flores-Carreón, A., Estrada-Mata, E., Mellado-Mojica, E., Németh, T., ... Mora-Montes, H. M. (2016). Role of protein glycosylation in Candida parapsilosis cell wall integrity and host interaction. Frontiers in Microbiology, 7(MAR), [306]. https://doi.org/10.3389/fmicb.2016.00306

Role of protein glycosylation in Candida parapsilosis cell wall integrity and host interaction. / Pérez-García, Luis A.; Csonka, Katalin; Flores-Carreón, Arturo; Estrada-Mata, Eine; Mellado-Mojica, Erika; Németh, Tibor; López-Ramírez, Luz A.; Toth, Renata; López, Mercedes G.; Vízler, C.; Marton, Annamaria; Tóth, Adél; Nosanchuk, Joshua D.; Gácser, A.; Mora-Montes, Héctor M.

In: Frontiers in Microbiology, Vol. 7, No. MAR, 306, 08.03.2016.

Research output: Contribution to journalArticle

Pérez-García, LA, Csonka, K, Flores-Carreón, A, Estrada-Mata, E, Mellado-Mojica, E, Németh, T, López-Ramírez, LA, Toth, R, López, MG, Vízler, C, Marton, A, Tóth, A, Nosanchuk, JD, Gácser, A & Mora-Montes, HM 2016, 'Role of protein glycosylation in Candida parapsilosis cell wall integrity and host interaction', Frontiers in Microbiology, vol. 7, no. MAR, 306. https://doi.org/10.3389/fmicb.2016.00306
Pérez-García LA, Csonka K, Flores-Carreón A, Estrada-Mata E, Mellado-Mojica E, Németh T et al. Role of protein glycosylation in Candida parapsilosis cell wall integrity and host interaction. Frontiers in Microbiology. 2016 Mar 8;7(MAR). 306. https://doi.org/10.3389/fmicb.2016.00306
Pérez-García, Luis A. ; Csonka, Katalin ; Flores-Carreón, Arturo ; Estrada-Mata, Eine ; Mellado-Mojica, Erika ; Németh, Tibor ; López-Ramírez, Luz A. ; Toth, Renata ; López, Mercedes G. ; Vízler, C. ; Marton, Annamaria ; Tóth, Adél ; Nosanchuk, Joshua D. ; Gácser, A. ; Mora-Montes, Héctor M. / Role of protein glycosylation in Candida parapsilosis cell wall integrity and host interaction. In: Frontiers in Microbiology. 2016 ; Vol. 7, No. MAR.
@article{a27b9bce68c84abb9545c399b8d3d395,
title = "Role of protein glycosylation in Candida parapsilosis cell wall integrity and host interaction",
abstract = "Candida parapsilosis is an important, emerging opportunistic fungal pathogen. Highly mannosylated fungal cell wall proteins are initial contact points with host immune systems. In Candida albicans, Och1 is a Golgi α1,6-mannosyltransferase that plays a key role in the elaboration of the N-linked mannan outer chain. Here, we disrupted C. parapsilosis OCH1 to gain insights into the contribution of N-linked mannosylation to cell fitness and to interactions with immune cells. Loss of Och1 in C. parapsilosis resulted in cellular aggregation, failure of morphogenesis, enhanced susceptibility to cell wall perturbing agents and defects in wall composition. We removed the cell wall O-linked mannans by β-elimination, and assessed the relevance of mannans during interaction with human monocytes. Results indicated that O-linked mannans are important for IL-1β stimulation in a dectin-1 and TLR4-dependent pathway; whereas both, N- and O-linked mannans are equally important ligands for TNFα and IL-6 stimulation, but neither is involved in IL-10 production. Furthermore, mice infected with C. parapsilosis och1Δ null mutant cells had significantly lower fungal burdens compared to wild-type (WT)-challenged counterparts. Therefore, our data are the first to demonstrate that C. parapsilosis N- and O-linked mannans have different roles in host interactions than those reported for C. albicans.",
keywords = "Candida parapsilosis, Cell wall, Host-fungus interplay, Mannosylation pathway, Mannosyltransferase, Virulence",
author = "P{\'e}rez-Garc{\'i}a, {Luis A.} and Katalin Csonka and Arturo Flores-Carre{\'o}n and Eine Estrada-Mata and Erika Mellado-Mojica and Tibor N{\'e}meth and L{\'o}pez-Ram{\'i}rez, {Luz A.} and Renata Toth and L{\'o}pez, {Mercedes G.} and C. V{\'i}zler and Annamaria Marton and Ad{\'e}l T{\'o}th and Nosanchuk, {Joshua D.} and A. G{\'a}cser and Mora-Montes, {H{\'e}ctor M.}",
year = "2016",
month = "3",
day = "8",
doi = "10.3389/fmicb.2016.00306",
language = "English",
volume = "7",
journal = "Frontiers in Microbiology",
issn = "1664-302X",
publisher = "Frontiers Media S. A.",
number = "MAR",

}

TY - JOUR

T1 - Role of protein glycosylation in Candida parapsilosis cell wall integrity and host interaction

AU - Pérez-García, Luis A.

AU - Csonka, Katalin

AU - Flores-Carreón, Arturo

AU - Estrada-Mata, Eine

AU - Mellado-Mojica, Erika

AU - Németh, Tibor

AU - López-Ramírez, Luz A.

AU - Toth, Renata

AU - López, Mercedes G.

AU - Vízler, C.

AU - Marton, Annamaria

AU - Tóth, Adél

AU - Nosanchuk, Joshua D.

AU - Gácser, A.

AU - Mora-Montes, Héctor M.

PY - 2016/3/8

Y1 - 2016/3/8

N2 - Candida parapsilosis is an important, emerging opportunistic fungal pathogen. Highly mannosylated fungal cell wall proteins are initial contact points with host immune systems. In Candida albicans, Och1 is a Golgi α1,6-mannosyltransferase that plays a key role in the elaboration of the N-linked mannan outer chain. Here, we disrupted C. parapsilosis OCH1 to gain insights into the contribution of N-linked mannosylation to cell fitness and to interactions with immune cells. Loss of Och1 in C. parapsilosis resulted in cellular aggregation, failure of morphogenesis, enhanced susceptibility to cell wall perturbing agents and defects in wall composition. We removed the cell wall O-linked mannans by β-elimination, and assessed the relevance of mannans during interaction with human monocytes. Results indicated that O-linked mannans are important for IL-1β stimulation in a dectin-1 and TLR4-dependent pathway; whereas both, N- and O-linked mannans are equally important ligands for TNFα and IL-6 stimulation, but neither is involved in IL-10 production. Furthermore, mice infected with C. parapsilosis och1Δ null mutant cells had significantly lower fungal burdens compared to wild-type (WT)-challenged counterparts. Therefore, our data are the first to demonstrate that C. parapsilosis N- and O-linked mannans have different roles in host interactions than those reported for C. albicans.

AB - Candida parapsilosis is an important, emerging opportunistic fungal pathogen. Highly mannosylated fungal cell wall proteins are initial contact points with host immune systems. In Candida albicans, Och1 is a Golgi α1,6-mannosyltransferase that plays a key role in the elaboration of the N-linked mannan outer chain. Here, we disrupted C. parapsilosis OCH1 to gain insights into the contribution of N-linked mannosylation to cell fitness and to interactions with immune cells. Loss of Och1 in C. parapsilosis resulted in cellular aggregation, failure of morphogenesis, enhanced susceptibility to cell wall perturbing agents and defects in wall composition. We removed the cell wall O-linked mannans by β-elimination, and assessed the relevance of mannans during interaction with human monocytes. Results indicated that O-linked mannans are important for IL-1β stimulation in a dectin-1 and TLR4-dependent pathway; whereas both, N- and O-linked mannans are equally important ligands for TNFα and IL-6 stimulation, but neither is involved in IL-10 production. Furthermore, mice infected with C. parapsilosis och1Δ null mutant cells had significantly lower fungal burdens compared to wild-type (WT)-challenged counterparts. Therefore, our data are the first to demonstrate that C. parapsilosis N- and O-linked mannans have different roles in host interactions than those reported for C. albicans.

KW - Candida parapsilosis

KW - Cell wall

KW - Host-fungus interplay

KW - Mannosylation pathway

KW - Mannosyltransferase

KW - Virulence

UR - http://www.scopus.com/inward/record.url?scp=84964402685&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84964402685&partnerID=8YFLogxK

U2 - 10.3389/fmicb.2016.00306

DO - 10.3389/fmicb.2016.00306

M3 - Article

VL - 7

JO - Frontiers in Microbiology

JF - Frontiers in Microbiology

SN - 1664-302X

IS - MAR

M1 - 306

ER -