Expression and processing of Plasmodium berghei SERA3 during liver stages.

Anja Schmidt-Christensen; Angelika Sturm; Sebastian Horstmann; Volker Heussler

doi:10.1111/j.1462-5822.2008.01162.x

Expression and processing of Plasmodium berghei SERA3 during liver stages.

Anja Schmidt-Christensen, Angelika Sturm, Sebastian Horstmann, Volker Heussler

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

48 Citationer (Scopus)

118 Downloads (Pure)

Abstract

Udgivelsesdato: 7 May 2008

Originalsprog	Engelsk
Tidsskrift	Cellular Microbiology
Vol/bind	10
Udgave nummer	8
Sider (fra-til)	1723-34
Antal sider	12
ISSN	1462-5814
DOI	https://doi.org/10.1111/j.1462-5822.2008.01162.x
Status	Udgivet - 2008
Udgivet eksternt	Ja

Bibliografisk note

Paper id:: PMID: 18419771

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10.1111/j.1462-5822.2008.01162.x

Schmidt-Christensen 2008Forlagets udgivne version, 0,99 MB

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Citationsformater

@article{4fbf49d0223d11df8ed1000ea68e967b,

title = "Expression and processing of Plasmodium berghei SERA3 during liver stages.",

abstract = "Cysteine proteases mediate liberation of Plasmodium berghei merozoites from infected hepatocytes. In an attempt to identify the responsible parasite proteases, we screened the genome of P. berghei for cysteine protease-encoding genes. RT-PCR analyses revealed that transcription of four out of five P. berghei serine repeat antigen (PbSERA) genes was strongly upregulated in late liver stages briefly before the parasitophorous vacuole membrane ruptured to release merozoites into the host cell cytoplasm, suggesting a role of PbSERA proteases in these processes. In order to characterize PbSERA3 processing, we raised an antiserum against a non-conserved region of the protein and generated a transgenic P. berghei strain expressing a TAP-tagged PbSERA3 under the control of the endogenous promoter. Immunofluorescence assays revealed that PbSERA3 leaks into the host cell cytoplasm during merozoite development, where it might contribute to host cell death or activate host cell proteases that execute cell death. Importantly, processed PbSERA3 has been detected by Western blot analysis in cell extracts of schizont-infected cells and merozoite-infected detached hepatic cells.",

author = "Anja Schmidt-Christensen and Angelika Sturm and Sebastian Horstmann and Volker Heussler",

note = "Paper id:: PMID: 18419771",

year = "2008",

doi = "10.1111/j.1462-5822.2008.01162.x",

language = "English",

volume = "10",

pages = "1723--34",

journal = "Cellular Microbiology",

issn = "1462-5814",

publisher = "Wiley-Blackwell",

number = "8",

}

TY - JOUR

T1 - Expression and processing of Plasmodium berghei SERA3 during liver stages.

AU - Schmidt-Christensen, Anja

AU - Sturm, Angelika

AU - Horstmann, Sebastian

AU - Heussler, Volker

N1 - Paper id:: PMID: 18419771

PY - 2008

Y1 - 2008

N2 - Cysteine proteases mediate liberation of Plasmodium berghei merozoites from infected hepatocytes. In an attempt to identify the responsible parasite proteases, we screened the genome of P. berghei for cysteine protease-encoding genes. RT-PCR analyses revealed that transcription of four out of five P. berghei serine repeat antigen (PbSERA) genes was strongly upregulated in late liver stages briefly before the parasitophorous vacuole membrane ruptured to release merozoites into the host cell cytoplasm, suggesting a role of PbSERA proteases in these processes. In order to characterize PbSERA3 processing, we raised an antiserum against a non-conserved region of the protein and generated a transgenic P. berghei strain expressing a TAP-tagged PbSERA3 under the control of the endogenous promoter. Immunofluorescence assays revealed that PbSERA3 leaks into the host cell cytoplasm during merozoite development, where it might contribute to host cell death or activate host cell proteases that execute cell death. Importantly, processed PbSERA3 has been detected by Western blot analysis in cell extracts of schizont-infected cells and merozoite-infected detached hepatic cells.

AB - Cysteine proteases mediate liberation of Plasmodium berghei merozoites from infected hepatocytes. In an attempt to identify the responsible parasite proteases, we screened the genome of P. berghei for cysteine protease-encoding genes. RT-PCR analyses revealed that transcription of four out of five P. berghei serine repeat antigen (PbSERA) genes was strongly upregulated in late liver stages briefly before the parasitophorous vacuole membrane ruptured to release merozoites into the host cell cytoplasm, suggesting a role of PbSERA proteases in these processes. In order to characterize PbSERA3 processing, we raised an antiserum against a non-conserved region of the protein and generated a transgenic P. berghei strain expressing a TAP-tagged PbSERA3 under the control of the endogenous promoter. Immunofluorescence assays revealed that PbSERA3 leaks into the host cell cytoplasm during merozoite development, where it might contribute to host cell death or activate host cell proteases that execute cell death. Importantly, processed PbSERA3 has been detected by Western blot analysis in cell extracts of schizont-infected cells and merozoite-infected detached hepatic cells.

U2 - 10.1111/j.1462-5822.2008.01162.x

DO - 10.1111/j.1462-5822.2008.01162.x

M3 - Journal article

C2 - 18419771

SN - 1462-5814

VL - 10

SP - 1723

EP - 1734

JO - Cellular Microbiology

JF - Cellular Microbiology

IS - 8

ER -