Computer analysis of antigenic domains and RGD-like sequences (RGWG) in the E glycoprotein of flaviviruses: An approach to vaccine development

Becker, Yechiel

doi:10.1007/bf00265636

Cited by 7 publications

(1 citation statement)

References 27 publications

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“…The first important receptor–ligand interaction involves integrins, which are known to play the role of surface cell receptors. This proposition has been put forward after the discovery of the RGD (Arg‐Gly‐Asp), or RGD‐like, motives in amino acid sequences of domain III of protein E of certain flaviviruses (Becker, ; Lobigs et al ., ; van der Most et al ., ). Lately, the importance of integrins for the process of flavivirus virion–cell integration has been confirmed experimentally (Chu and Ng, ; Lee et al ., ).…”

Section: Introductionmentioning

confidence: 99%

Force‐induced globule–coil transition in laminin binding protein and its role for viral–cell membrane fusion

Зайцев

Benedetti

Mikhaylov

et al. 2014

J of Molecular Recognition

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The specific interactions of the pairs laminin binding protein (LBP)-purified tick-borne encephalitis viral surface protein E and certain recombinant fragments of this protein, as well as West Nile viral surface protein E and certain recombinant fragments of that protein, are studied by combined methods of single-molecule dynamic force spectroscopy (SMDFS), enzyme immunoassay and optical surface waves-based biosensor measurements. The experiments were performed at neutral pH (7.4) and acid pH (5.3) conditions. The data obtained confirm the role of LBP as a cell receptor for two typical viral species of the Flavivirus genus. A comparison of these data with similar data obtained for another cell receptor of this family, namely human αVβ3 integrin, reveals that both these receptors are very important. Studying the specific interaction between the cell receptors in question and specially prepared monoclonal antibodies against them, we could show that both interaction sites involved in the process of virus-cell interaction remain intact at pH 5.3. At the same time, for these acid conditions characteristic for an endosome during flavivirus-cell membrane fusion, SMDFS data reveal the existence of a force-induced (effective already for forces as small as 30-70 pN) sharp globule-coil transition for LBP and LBP-fragments of protein E complexes. We argue that this conformational transformation, being an analog of abrupt first-order phase transition and having similarity with the famous Rayleigh hydrodynamic instability, might be indispensable for the flavivirus-cell membrane fusion process.

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Section: Introductionmentioning

confidence: 99%

Force‐induced globule–coil transition in laminin binding protein and its role for viral–cell membrane fusion

Зайцев

Benedetti

Mikhaylov

et al. 2014

J of Molecular Recognition

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The pharmacology of the integrins

Cox

Aoki

Seki

et al. 1994

Medicinal Research Reviews

121

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Computer prediction of antigenic and topogenic domains in HSV-1 and HSV-2 glycoprotein B (gB)

Becker

1992

Virus Genes

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The envelope glycoprotein B (gB) coded for by the herpes simplex virus type 1 (HSV-1) UL27 gene is similar to the amino acid (aa) sequence of the gB coded by a homologous gene in HSV-2 DNA. The putative antigenic domains in HSV-1 and HSV-2 gB glycoproteins were analyzed on a comparative basis by suitable computer programs, which allowed the prediction of putative antigenic and topogenic domains. The computer-derived domains were compared to experimentally reported antigenic domains in HSV-1 gB glycoprotein. The computer-predicted antigenic domains in the HSV-1 gB glycoprotein matched well with the reported experimentally derived antigenic domains. The aa sequence of antigenic domain 1 was noted to resemble the amino acid sequence in ApoE that is involved in the attachment of this protein to LDL receptors. The clusters of hydrophobic aa domains are conserved in the two viral glycoproteins and are signals for transfer of the viral proteins through the cellular membrane.

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Computer analysis of antigenic domains and RGD-like sequences (RGWG) in the E glycoprotein of flaviviruses: An approach to vaccine development

Cited by 7 publications

References 27 publications

Force‐induced globule–coil transition in laminin binding protein and its role for viral–cell membrane fusion

Force‐induced globule–coil transition in laminin binding protein and its role for viral–cell membrane fusion

The pharmacology of the integrins

Computer prediction of antigenic and topogenic domains in HSV-1 and HSV-2 glycoprotein B (gB)

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