Novel interactions of domain III from the envelope glycoprotein of dengue 2 virus with human plasma proteins

Huerta, Vivian; Ramos, Yassel; Yero, Alexis; Martin, Dayron; Toledo, Patricia; Fleitas, Noralvis; Gallien, Sébastien; Martín, Alejandro; Márquez, Gabriel; Pérez-Riverol, Yasset; Sarría, Mónica; Guirola, Osmany; González, Luis Javier; Domon, Bruno; Chinea, Glay

doi:10.1016/j.jprot.2015.11.003

Cited by 15 publications

(9 citation statements)

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“…The DENV E protein mediates virus receptor binding (REF) and a number of DENV E cell surface expressed receptor binding proteins have been identified (reviewed in [ 32 , 33 ]). More recently an interactomic analysis of blood plasma proteins identified 27 plasma proteins capable of interacting with domain III of DENV E protein [ 34 ]. However, to date, only a few intracellular interactions between DENV E protein and cytosolic proteins have been described.…”

Section: Discussionmentioning

confidence: 99%

Actin Interacts with Dengue Virus 2 and 4 Envelope Proteins

et al. 2016

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Dengue virus (DENV) remains a significant public health problem in many tropical and sub-tropical countries worldwide. The DENV envelope (E) protein is the major antigenic determinant and the protein that mediates receptor binding and endosomal fusion. In contrast to some other DENV proteins, relatively few cellular interacting proteins have been identified. To address this issue a co-immuoprecipitation strategy was employed. The predominant co-immunoprecipitating proteins identified were actin and actin related proteins, however the results suggested that actin was the only bona fide interacting partner. Actin was shown to interact with the E protein of DENV 2 and 4, and the interaction between actin and DENV E protein was shown to occur in a truncated DENV consisting of only domains I and II. Actin was shown to decrease during infection, but this was not associated with a decrease in gene transcription. Actin-related proteins also showed a decrease in expression during infection that was not transcriptionally regulated. Cytoskeletal reorganization was not observed during infection, suggesting that the interaction between actin and E protein has a cell type specific component.

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Section: Discussionmentioning

confidence: 99%

Actin Interacts with Dengue Virus 2 and 4 Envelope Proteins

et al. 2016

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“…Then, the column was washed sequentially with preparations of equilibration buffer containing increasing concentrations of NaCl (0.3 M, 0.6 M and 1 M) at 30 cm/h, and the protein species still bound to the column afterwards were eluted by the successive application of 0.02 M sodium acetate pH 3.0, water and 0.01 M NaOH. Chromatography fractions were used either separately or pooled in a single sample (ELU AXC ) [2] ( Fig. 1 ).…”

Section: Fractionation Of Human Plasma Samplesmentioning

confidence: 99%

Dataset on protein composition of a human plasma sub-proteome able to modulate the Dengue 2 virus infection in Huh 7.5 cells

et al. 2016

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The four serotypes of dengue virus (DENV1-4) are the causal agents of the emerging disease Dengue Fever and its severe forms. DENV is inoculated into human blood through a mosquito bite. Thus, plasma is an important media for DENV dissemination in infected persons and several important interactions should take place for the virus with human plasma proteins that strongly influence or may determine the course of the infection. This dataset contains 239 proteins identified in the elution fractions of human plasma subjected to DE-52 anion exchange chromatography. Data on DENV2 infection of Huh 7.5 cells in presence of the human plasma fraction is also presented.

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“…reported a direct binding of C1q to recombinant E protein of DENV and viral particles ( 21 ). This finding was confirmed by proteomic analysis demonstrating that samples from DENV-infected patients as well as purified domain III of DENV envelope protein bind several complement components among which C1q ( 22 , 23 ). As in addition, binding of C1q to NS1 of DENV is described ( 24 ), we tested the possibility of a direct interaction of C1q with viral particles and purified recombinant NS1 and E proteins of ZIKV.…”

Section: Discussionmentioning

confidence: 63%

Active Human Complement Reduces the Zika Virus Load via Formation of the Membrane-Attack Complex

et al. 2018

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Although neglected in the past, the interest on Zika virus (ZIKV) raised dramatically in the last several years. The rapid spread of the virus in Latin America and the association of the infection with microcephaly in newborns or Guillain-Barré Syndrome in adults prompted the WHO to declare the ZIKV epidemic to be an international public health emergency in 2016. As the virus gained only limited attention in the past, investigations on interactions of ZIKV with human complement are limited. This prompted us to investigate the stability of the virus to human complement. At low serum concentrations (10%) which refers to complement concentrations found on mucosal surfaces, the virus was relatively stable at 37°C, while at high complement levels (50% serum concentration) ZIKV titers were dramatically reduced, although the virus remained infectious for about 4–5 min under these conditions. The classical pathway was identified as the main actor of complement activation driven by IgM antibodies. In addition, direct binding of C1q to both envelope and NS1 proteins was observed. Formation of the MAC on the viral surface and thus complement-mediated lysis and not opsonization seems to be essential for the reduction of viral titers.

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Novel interactions of domain III from the envelope glycoprotein of dengue 2 virus with human plasma proteins

Cited by 15 publications

References 52 publications

Actin Interacts with Dengue Virus 2 and 4 Envelope Proteins

Actin Interacts with Dengue Virus 2 and 4 Envelope Proteins

Dataset on protein composition of a human plasma sub-proteome able to modulate the Dengue 2 virus infection in Huh 7.5 cells

Active Human Complement Reduces the Zika Virus Load via Formation of the Membrane-Attack Complex

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