Multiple Plasmodium falciparum erythrocyte membrane protein 1 variants per genome can bind IgM via its Fc fragment Fcμ

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Multiple Plasmodium falciparum erythrocyte membrane protein 1 variants per genome can bind IgM via its Fc fragment Fcμ. / Jeppesen, Anine; Ditlev, Sisse Bolm; Soroka, Vladyslav; Stevenson, Elisabeth Kay; Turner, Louise; Dzikowski, Ron; Hviid, Lars; Barfod, Lea.

In: Infection and Immunity, Vol. 83, No. 10, 2015, p. 3972-81.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Jeppesen, A, Ditlev, SB, Soroka, V, Stevenson, EK, Turner, L, Dzikowski, R, Hviid, L & Barfod, L 2015, 'Multiple Plasmodium falciparum erythrocyte membrane protein 1 variants per genome can bind IgM via its Fc fragment Fcμ', Infection and Immunity, vol. 83, no. 10, pp. 3972-81. https://doi.org/10.1128/IAI.00337-15

APA

Jeppesen, A., Ditlev, S. B., Soroka, V., Stevenson, E. K., Turner, L., Dzikowski, R., Hviid, L., & Barfod, L. (2015). Multiple Plasmodium falciparum erythrocyte membrane protein 1 variants per genome can bind IgM via its Fc fragment Fcμ. Infection and Immunity, 83(10), 3972-81. https://doi.org/10.1128/IAI.00337-15

Vancouver

Jeppesen A, Ditlev SB, Soroka V, Stevenson EK, Turner L, Dzikowski R et al. Multiple Plasmodium falciparum erythrocyte membrane protein 1 variants per genome can bind IgM via its Fc fragment Fcμ. Infection and Immunity. 2015;83(10):3972-81. https://doi.org/10.1128/IAI.00337-15

Author

Jeppesen, Anine ; Ditlev, Sisse Bolm ; Soroka, Vladyslav ; Stevenson, Elisabeth Kay ; Turner, Louise ; Dzikowski, Ron ; Hviid, Lars ; Barfod, Lea. / Multiple Plasmodium falciparum erythrocyte membrane protein 1 variants per genome can bind IgM via its Fc fragment Fcμ. In: Infection and Immunity. 2015 ; Vol. 83, No. 10. pp. 3972-81.

Bibtex

@article{8dbdcdbafeec405a92cbc48343008c04,
title = "Multiple Plasmodium falciparum erythrocyte membrane protein 1 variants per genome can bind IgM via its Fc fragment Fcμ",
abstract = "The Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) adhesive proteins expressed on the surfaces of infected erythrocytes (IEs) are of key importance in the pathogenesis of P. falciparum malaria. Several structurally and functionally defined PfEMP1 types have been associated with severe clinical manifestations, such as cerebral malaria in children and placental malaria in pregnant women. PfEMP1 that can bind the Fc part of IgM (Fcμ) characterizes one such type, although the functional significance of this IgM binding to PfEMP1 remains unclear. In this study, we report the identification and functional analysis of five IgM-binding PfEMP1 proteins encoded by P. falciparum NF54. In addition to the VAR2CSA-type PFL0030c protein, already known to bind Fcμ and to mediate chondroitin sulfate A (CSA)-specific adhesion of IEs in the placenta, we found four PfEMP1 proteins not previously known to bind IgM this way. Although they all contained Duffy binding-like ε (DBLε) domains similar to those in VAR2CSA-type PfEMP1, they did not mediate IE adhesion to CSA, and IgM binding did not shield IEs from phagocytosis of IgG-opsonized IEs. In this way, these new IgM-binding PfEMP1 proteins resemble the rosette-mediating and IgM-binding PfEMP1 HB3VAR06, but none of them mediated formation of rosettes. We could map the capacity for Fc-specific IgM binding to DBLε domains near the C terminus for three of the four PfEMP1 proteins tested. Our study provides new evidence regarding Fc-dependent binding of IgM to PfEMP1, which appears to be a common and multifunctional phenotype.",
author = "Anine Jeppesen and Ditlev, {Sisse Bolm} and Vladyslav Soroka and Stevenson, {Elisabeth Kay} and Louise Turner and Ron Dzikowski and Lars Hviid and Lea Barfod",
note = "Copyright {\textcopyright} 2015, Jeppesen et al.",
year = "2015",
doi = "10.1128/IAI.00337-15",
language = "English",
volume = "83",
pages = "3972--81",
journal = "Infection and Immunity",
issn = "0019-9567",
publisher = "American Society for Microbiology",
number = "10",

}

RIS

TY - JOUR

T1 - Multiple Plasmodium falciparum erythrocyte membrane protein 1 variants per genome can bind IgM via its Fc fragment Fcμ

AU - Jeppesen, Anine

AU - Ditlev, Sisse Bolm

AU - Soroka, Vladyslav

AU - Stevenson, Elisabeth Kay

AU - Turner, Louise

AU - Dzikowski, Ron

AU - Hviid, Lars

AU - Barfod, Lea

N1 - Copyright © 2015, Jeppesen et al.

PY - 2015

Y1 - 2015

N2 - The Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) adhesive proteins expressed on the surfaces of infected erythrocytes (IEs) are of key importance in the pathogenesis of P. falciparum malaria. Several structurally and functionally defined PfEMP1 types have been associated with severe clinical manifestations, such as cerebral malaria in children and placental malaria in pregnant women. PfEMP1 that can bind the Fc part of IgM (Fcμ) characterizes one such type, although the functional significance of this IgM binding to PfEMP1 remains unclear. In this study, we report the identification and functional analysis of five IgM-binding PfEMP1 proteins encoded by P. falciparum NF54. In addition to the VAR2CSA-type PFL0030c protein, already known to bind Fcμ and to mediate chondroitin sulfate A (CSA)-specific adhesion of IEs in the placenta, we found four PfEMP1 proteins not previously known to bind IgM this way. Although they all contained Duffy binding-like ε (DBLε) domains similar to those in VAR2CSA-type PfEMP1, they did not mediate IE adhesion to CSA, and IgM binding did not shield IEs from phagocytosis of IgG-opsonized IEs. In this way, these new IgM-binding PfEMP1 proteins resemble the rosette-mediating and IgM-binding PfEMP1 HB3VAR06, but none of them mediated formation of rosettes. We could map the capacity for Fc-specific IgM binding to DBLε domains near the C terminus for three of the four PfEMP1 proteins tested. Our study provides new evidence regarding Fc-dependent binding of IgM to PfEMP1, which appears to be a common and multifunctional phenotype.

AB - The Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) adhesive proteins expressed on the surfaces of infected erythrocytes (IEs) are of key importance in the pathogenesis of P. falciparum malaria. Several structurally and functionally defined PfEMP1 types have been associated with severe clinical manifestations, such as cerebral malaria in children and placental malaria in pregnant women. PfEMP1 that can bind the Fc part of IgM (Fcμ) characterizes one such type, although the functional significance of this IgM binding to PfEMP1 remains unclear. In this study, we report the identification and functional analysis of five IgM-binding PfEMP1 proteins encoded by P. falciparum NF54. In addition to the VAR2CSA-type PFL0030c protein, already known to bind Fcμ and to mediate chondroitin sulfate A (CSA)-specific adhesion of IEs in the placenta, we found four PfEMP1 proteins not previously known to bind IgM this way. Although they all contained Duffy binding-like ε (DBLε) domains similar to those in VAR2CSA-type PfEMP1, they did not mediate IE adhesion to CSA, and IgM binding did not shield IEs from phagocytosis of IgG-opsonized IEs. In this way, these new IgM-binding PfEMP1 proteins resemble the rosette-mediating and IgM-binding PfEMP1 HB3VAR06, but none of them mediated formation of rosettes. We could map the capacity for Fc-specific IgM binding to DBLε domains near the C terminus for three of the four PfEMP1 proteins tested. Our study provides new evidence regarding Fc-dependent binding of IgM to PfEMP1, which appears to be a common and multifunctional phenotype.

U2 - 10.1128/IAI.00337-15

DO - 10.1128/IAI.00337-15

M3 - Journal article

C2 - 26216422

VL - 83

SP - 3972

EP - 3981

JO - Infection and Immunity

JF - Infection and Immunity

SN - 0019-9567

IS - 10

ER -

ID: 144045157