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Träfflista för sökning "WFRF:(Wahlgren M) ;conttype:(refereed);pers:(Jiang N)"

Search: WFRF:(Wahlgren M) > Peer-reviewed > Jiang N

  • Result 1-9 of 9
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  • Chang, ZG, et al. (author)
  • The TatD-like DNase of Plasmodium is a virulence factor and a potential malaria vaccine candidate
  • 2016
  • In: Nature communications. - : Springer Science and Business Media LLC. - 2041-1723. ; 7, s. 11537-
  • Journal article (peer-reviewed)abstract
    • Neutrophil extracellular traps (NETs), composed primarily of DNA and proteases, are released from activated neutrophils and contribute to the innate immune response by capturing pathogens. Plasmodium falciparum, the causative agent of severe malaria, thrives in its host by counteracting immune elimination. Here, we report the discovery of a novel virulence factor of P. falciparum, a TatD-like DNase (PfTatD) that is expressed primarily in the asexual blood stage and is likely utilized by the parasite to counteract NETs. PfTatD exhibits typical deoxyribonuclease activity, and its expression is higher in virulent parasites than in avirulent parasites. A P. berghei TatD-knockout parasite displays reduced pathogenicity in mice. Mice immunized with recombinant TatD exhibit increased immunity against lethal challenge. Our results suggest that the TatD-like DNase is an essential factor for the survival of malarial parasites in the host and is a potential malaria vaccine candidate.
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  • Nilsson, S, et al. (author)
  • Characterization of the Duffy-Binding-Like Domain of Plasmodium falciparum Blood-Stage Antigen 332
  • 2011
  • In: Malaria research and treatment. - : Hindawi Limited. - 2044-4362. ; 2011, s. 671439-
  • Journal article (peer-reviewed)abstract
    • Studies on Pf332, a major Plasmodium falciparum blood-stage antigen, have largely been hampered by the cross-reactive nature of antibodies generated against the molecule due to its high content of repeats, which are present in other malaria antigens. We previously reported the identification of a conserved domain in Pf332 with a high degree of similarity to the Duffy-binding-like (DBL) domains of the erythrocyte-binding-like (EBL) family. We here describe that antibodies towards Pf332-DBL are induced after repeated exposure to P. falciparum and that they are acquired early in life in areas of intense malaria transmission. Furthermore, a homology model of Pf332-DBL was found to be similar to the structure of the EBL-DBLs. Despite their similarities, antibodies towards Pf332-DBL did not display any cross-reactivity with EBL-proteins as demonstrated by immunofluorescence microscopy, Western blotting, and peptide microarray. Thus the DBL domain is an attractive region to use in further studies on the giant Pf332 molecule.
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  • Result 1-9 of 9
Type of publication
journal article (9)
Type of content
Author/Editor
Wahlgren, M (9)
Chen, QJ (8)
Lu, HJ (7)
Yin, JG (5)
Chang, ZG (3)
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Zhang, Y. (2)
Nilsson, S. (2)
Yu, SC (2)
Zhang, YN (2)
Sun, X. (1)
Zhao, X. (1)
Song, M. (1)
Wang, Y. (1)
Wang, W. (1)
Zhang, K. (1)
Chen, Q. (1)
Berzins, K (1)
Moll, K (1)
Albrecht, L (1)
Angeletti, D (1)
Zhang, YY (1)
Cheng, XJ (1)
Zhang, ZX (1)
Zhang, DC (1)
Zhou, JH (1)
Feng, Y. (1)
Yang, N (1)
Huang, P (1)
Cao, YM (1)
Wei, XY (1)
Wang, DW (1)
Tu, ZW (1)
Du, C. (1)
Cai, PF (1)
Sang, XY (1)
Chang, QC (1)
Sun, XD (1)
Kursula, I (1)
Wang, HN (1)
Hou, N. (1)
Jia, BY (1)
Piao, XY (1)
Wang, HA (1)
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University
Karolinska Institutet (9)
Language
English (9)
Research subject (UKÄ/SCB)
Medical and Health Sciences (1)

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