Henipaviruses: recent observations on regulation of transcription and the nature of the cell receptor
Identifieur interne :
001396 ( PascalFrancis/Curation );
précédent :
001395;
suivant :
001397
Henipaviruses: recent observations on regulation of transcription and the nature of the cell receptor
Auteurs : B. T. Eaton [
Australie] ;
P. J. Wright [
Australie] ;
L.-F. Wang [
Australie] ;
O. Sergeyev [
Australie] ;
W. P. Michalski [
Australie] ;
K. N. Bossart [
États-Unis] ;
C. C. Broder [
États-Unis]
Source :
-
Archives of virology. Supplementum [ 0939-1983 ] ; 2004.
RBID : Pascal:04-0472244
Descripteurs français
English descriptors
Abstract
Hendra virus (HENV) and Nipah virus (NIPV) are classified in the new genus Henipavirus, within the subfamily Paramyxovirinae, family Paramyxoviridae. The genetic and biological characteristics that differentiate henipaviruses from other members of the subfamily are summarized. Although they do not display neuraminidase and hemagglutination activities and in that regard resemble viruses in the genus Morbillivirus, several recent observations highlight similarities between henipaviruses and respiroviruses (genus Respirovirus) in structure and replication strategy. First, three-dimensional modeling studies suggest that the external globular head domain of the HENV G protein resembles that of respiroviruses rather than morbilliviruses. Second, the pattern of transcriptional attenuation in HENV-infected cells resembles that observed with Sendai virus, a respirovirus, and differs from that found in cells infected with measles virus, a morbillivirus. Henipaviruses have a broad host range in vitro and in vivo, indicating wide distribution of cellular receptor molecules. The extensive host range has been confirmed in a quantitative in vitro cell-fusion assay using recombinant vaccinia viruses expressing the attachment and fusion proteins of HENV and NIPV. Cell lines of diverse origin and which are permissive in the in vitro cell fusion assay have been identified and the pattern of relative susceptibilities is the same for both HENV and NIPV, implying that both viruses use the same cell receptor. Protease treatment of permissive cells destroys their ability to fuse with cells expressing viral envelope glycoproteins. Virus overlay protein binding assay (VOPBA) and radio-immune precipitation assays confirm that both HENV and NIPV bind to membrane proteins in the 35-50 kD range. Treatment of cell membrane proteins with N-glycosidase eliminates HeV binding activity in VOPBA whereas treatment with neuraminidase has no effect on binding. Thus preliminary evidence suggests that NIPV and HENV bind to the same glycoprotein receptor via a non-sialic acid-dependant mechanism.
| pA |
| A01 | 01 | 1 | | @0 0939-1983 |
|---|
| A03 | | 1 | | @0 Arch. virol., Suppl. |
|---|
| A06 | | | | @2 18 |
|---|
| A08 | 01 | 1 | ENG | @1 Henipaviruses: recent observations on regulation of transcription and the nature of the cell receptor |
|---|
| A09 | 01 | 1 | ENG | @1 Emergence and control of zoonotic viral encephalitides |
|---|
| A11 | 01 | 1 | | @1 EATON (B. T.) |
|---|
| A11 | 02 | 1 | | @1 WRIGHT (P. J.) |
|---|
| A11 | 03 | 1 | | @1 WANG (L.-F.) |
|---|
| A11 | 04 | 1 | | @1 SERGEYEV (O.) |
|---|
| A11 | 05 | 1 | | @1 MICHALSKI (W. P.) |
|---|
| A11 | 06 | 1 | | @1 BOSSART (K. N.) |
|---|
| A11 | 07 | 1 | | @1 BRODER (C. C.) |
|---|
| A12 | 01 | 1 | | @1 CALISHER (Charles H.) @9 ed. |
|---|
| A12 | 02 | 1 | | @1 GRIFFIN (Diane E.) @9 ed. |
|---|
| A14 | 01 | | | @1 Australian Animal Health Laboratory, CSIRO Livestock Industries @2 Geelong @3 AUS @Z 1 aut. @Z 3 aut. @Z 4 aut. @Z 5 aut. |
|---|
| A14 | 02 | | | @1 Department of Microbiology, Monash University @2 Clayton @3 AUS @Z 2 aut. |
|---|
| A14 | 03 | | | @1 Department of Microbiology, Uniformed Services University @2 Bethesda, Maryland @3 USA @Z 6 aut. @Z 7 aut. |
|---|
| A18 | 01 | 1 | | @1 Mérieux Foundation @2 Lyon @3 FRA @9 patr. |
|---|
| A20 | | | | @1 123-131 |
|---|
| A21 | | | | @1 2004 |
|---|
| A23 | 01 | | | @0 ENG |
|---|
| A43 | 01 | | | @1 INIST @2 6355S @5 354000117181120100 |
|---|
| A44 | | | | @0 0000 @1 © 2004 INIST-CNRS. All rights reserved. |
|---|
| A45 | | | | @0 32 ref. |
|---|
| A47 | 01 | 1 | | @0 04-0472244 |
|---|
| A60 | | | | @1 P @2 C |
|---|
| A61 | | | | @0 A |
|---|
| A64 | 01 | 1 | | @0 Archives of virology. Supplementum |
|---|
| A66 | 01 | | | @0 AUT |
|---|
| C01 | 01 | | ENG | @0 Hendra virus (HENV) and Nipah virus (NIPV) are classified in the new genus Henipavirus, within the subfamily Paramyxovirinae, family Paramyxoviridae. The genetic and biological characteristics that differentiate henipaviruses from other members of the subfamily are summarized. Although they do not display neuraminidase and hemagglutination activities and in that regard resemble viruses in the genus Morbillivirus, several recent observations highlight similarities between henipaviruses and respiroviruses (genus Respirovirus) in structure and replication strategy. First, three-dimensional modeling studies suggest that the external globular head domain of the HENV G protein resembles that of respiroviruses rather than morbilliviruses. Second, the pattern of transcriptional attenuation in HENV-infected cells resembles that observed with Sendai virus, a respirovirus, and differs from that found in cells infected with measles virus, a morbillivirus. Henipaviruses have a broad host range in vitro and in vivo, indicating wide distribution of cellular receptor molecules. The extensive host range has been confirmed in a quantitative in vitro cell-fusion assay using recombinant vaccinia viruses expressing the attachment and fusion proteins of HENV and NIPV. Cell lines of diverse origin and which are permissive in the in vitro cell fusion assay have been identified and the pattern of relative susceptibilities is the same for both HENV and NIPV, implying that both viruses use the same cell receptor. Protease treatment of permissive cells destroys their ability to fuse with cells expressing viral envelope glycoproteins. Virus overlay protein binding assay (VOPBA) and radio-immune precipitation assays confirm that both HENV and NIPV bind to membrane proteins in the 35-50 kD range. Treatment of cell membrane proteins with N-glycosidase eliminates HeV binding activity in VOPBA whereas treatment with neuraminidase has no effect on binding. Thus preliminary evidence suggests that NIPV and HENV bind to the same glycoprotein receptor via a non-sialic acid-dependant mechanism. |
|---|
| C02 | 01 | X | | @0 002A05C05 |
|---|
| C03 | 01 | X | FRE | @0 Paramyxoviridae @2 NW @5 01 |
|---|
| C03 | 01 | X | ENG | @0 Paramyxoviridae @2 NW @5 01 |
|---|
| C03 | 01 | X | SPA | @0 Paramyxoviridae @2 NW @5 01 |
|---|
| C03 | 02 | X | FRE | @0 Régulation @5 05 |
|---|
| C03 | 02 | X | ENG | @0 Regulation(control) @5 05 |
|---|
| C03 | 02 | X | SPA | @0 Regulación @5 05 |
|---|
| C03 | 03 | X | FRE | @0 Transcription @5 06 |
|---|
| C03 | 03 | X | ENG | @0 Transcription @5 06 |
|---|
| C03 | 03 | X | SPA | @0 Transcripción @5 06 |
|---|
| C03 | 04 | X | FRE | @0 Protéine @5 07 |
|---|
| C03 | 04 | X | ENG | @0 Protein @5 07 |
|---|
| C03 | 04 | X | SPA | @0 Proteína @5 07 |
|---|
| C03 | 05 | X | FRE | @0 Maladie émergente @2 NM @5 14 |
|---|
| C03 | 05 | X | ENG | @0 Emerging disease @2 NM @5 14 |
|---|
| C03 | 05 | X | SPA | @0 Enfermedad emergente @2 NM @5 14 |
|---|
| C03 | 06 | X | FRE | @0 Virus Nipah @4 INC @5 15 |
|---|
| C03 | 07 | X | FRE | @0 Virus Hendra @4 INC @5 79 |
|---|
| C07 | 01 | X | FRE | @0 Mononegavirales @2 NW |
|---|
| C07 | 01 | X | ENG | @0 Mononegavirales @2 NW |
|---|
| C07 | 01 | X | SPA | @0 Mononegavirales @2 NW |
|---|
| C07 | 02 | X | FRE | @0 Virus @2 NW |
|---|
| C07 | 02 | X | ENG | @0 Virus @2 NW |
|---|
| C07 | 02 | X | SPA | @0 Virus @2 NW |
|---|
| N21 | | | | @1 264 |
|---|
|
|---|
| pR |
| A30 | 01 | 1 | ENG | @1 Emergence and control of zoonotic viral encephalitis. Symposium @3 Veyrier du Lac FRA @4 2003-04-06 |
|---|
|
|---|
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Le document en format XML
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</publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a">Henipaviruses: recent observations on regulation of transcription and the nature of the cell receptor</title>
<author><name sortKey="Eaton, B T" sort="Eaton, B T" uniqKey="Eaton B" first="B. T." last="Eaton">B. T. Eaton</name>
<affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Australian Animal Health Laboratory, CSIRO Livestock Industries</s1>
<s2>Geelong</s2>
<s3>AUS</s3>
<sZ>1 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
</inist:fA14><country>Australie</country>
</affiliation><author><name sortKey="Wright, P J" sort="Wright, P J" uniqKey="Wright P" first="P. J." last="Wright">P. J. Wright</name>
<affiliation wicri:level="1"><inist:fA14 i1="02"><s1>Department of Microbiology, Monash University</s1>
<s2>Clayton</s2>
<s3>AUS</s3>
<sZ>2 aut.</sZ>
</inist:fA14><country>Australie</country>
</affiliation><author><name sortKey="Wang, L F" sort="Wang, L F" uniqKey="Wang L" first="L.-F." last="Wang">L.-F. Wang</name>
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<s2>Geelong</s2>
<s3>AUS</s3>
<sZ>1 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
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</affiliation><author><name sortKey="Sergeyev, O" sort="Sergeyev, O" uniqKey="Sergeyev O" first="O." last="Sergeyev">O. Sergeyev</name>
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<sZ>1 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
</inist:fA14><country>Australie</country>
</affiliation><author><name sortKey="Michalski, W P" sort="Michalski, W P" uniqKey="Michalski W" first="W. P." last="Michalski">W. P. Michalski</name>
<affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Australian Animal Health Laboratory, CSIRO Livestock Industries</s1>
<s2>Geelong</s2>
<s3>AUS</s3>
<sZ>1 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
</inist:fA14><country>Australie</country>
</affiliation><author><name sortKey="Bossart, K N" sort="Bossart, K N" uniqKey="Bossart K" first="K. N." last="Bossart">K. N. Bossart</name>
<affiliation wicri:level="1"><inist:fA14 i1="03"><s1>Department of Microbiology, Uniformed Services University</s1>
<s2>Bethesda, Maryland</s2>
<s3>USA</s3>
<sZ>6 aut.</sZ>
<sZ>7 aut.</sZ>
</inist:fA14><country>États-Unis</country>
</affiliation><author><name sortKey="Broder, C C" sort="Broder, C C" uniqKey="Broder C" first="C. C." last="Broder">C. C. Broder</name>
<affiliation wicri:level="1"><inist:fA14 i1="03"><s1>Department of Microbiology, Uniformed Services University</s1>
<s2>Bethesda, Maryland</s2>
<s3>USA</s3>
<sZ>6 aut.</sZ>
<sZ>7 aut.</sZ>
</inist:fA14><country>États-Unis</country>
</affiliation><series><title level="j" type="main">Archives of virology. Supplementum</title>
<title level="j" type="abbreviated">Arch. virol., Suppl.</title>
<idno type="ISSN">0939-1983</idno>
<imprint><date when="2004">2004</date>
</imprint><seriesStmt><title level="j" type="main">Archives of virology. Supplementum</title>
<title level="j" type="abbreviated">Arch. virol., Suppl.</title>
<idno type="ISSN">0939-1983</idno>
</seriesStmt><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Emerging disease</term>
<term>Paramyxoviridae</term>
<term>Protein</term>
<term>Regulation(control)</term>
<term>Transcription</term>
</keywords><keywords scheme="Pascal" xml:lang="fr"><term>Paramyxoviridae</term>
<term>Régulation</term>
<term>Transcription</term>
<term>Protéine</term>
<term>Maladie émergente</term>
<term>Virus Nipah</term>
<term>Virus Hendra</term>
</keywords><front><div type="abstract" xml:lang="en">Hendra virus (HENV) and Nipah virus (NIPV) are classified in the new genus Henipavirus, within the subfamily Paramyxovirinae, family Paramyxoviridae. The genetic and biological characteristics that differentiate henipaviruses from other members of the subfamily are summarized. Although they do not display neuraminidase and hemagglutination activities and in that regard resemble viruses in the genus Morbillivirus, several recent observations highlight similarities between henipaviruses and respiroviruses (genus Respirovirus) in structure and replication strategy. First, three-dimensional modeling studies suggest that the external globular head domain of the HENV G protein resembles that of respiroviruses rather than morbilliviruses. Second, the pattern of transcriptional attenuation in HENV-infected cells resembles that observed with Sendai virus, a respirovirus, and differs from that found in cells infected with measles virus, a morbillivirus. Henipaviruses have a broad host range in vitro and in vivo, indicating wide distribution of cellular receptor molecules. The extensive host range has been confirmed in a quantitative in vitro cell-fusion assay using recombinant vaccinia viruses expressing the attachment and fusion proteins of HENV and NIPV. Cell lines of diverse origin and which are permissive in the in vitro cell fusion assay have been identified and the pattern of relative susceptibilities is the same for both HENV and NIPV, implying that both viruses use the same cell receptor. Protease treatment of permissive cells destroys their ability to fuse with cells expressing viral envelope glycoproteins. Virus overlay protein binding assay (VOPBA) and radio-immune precipitation assays confirm that both HENV and NIPV bind to membrane proteins in the 35-50 kD range. Treatment of cell membrane proteins with N-glycosidase eliminates HeV binding activity in VOPBA whereas treatment with neuraminidase has no effect on binding. Thus preliminary evidence suggests that NIPV and HENV bind to the same glycoprotein receptor via a non-sialic acid-dependant mechanism.</div>
</front><inist><standard h6="B"><pA><fA01 i1="01" i2="1"><s0>0939-1983</s0>
</fA01><fA03 i2="1"><s0>Arch. virol., Suppl.</s0>
</fA03><fA08 i1="01" i2="1" l="ENG"><s1>Henipaviruses: recent observations on regulation of transcription and the nature of the cell receptor</s1>
</fA08><fA09 i1="01" i2="1" l="ENG"><s1>Emergence and control of zoonotic viral encephalitides</s1>
</fA09><fA11 i1="01" i2="1"><s1>EATON (B. T.)</s1>
</fA11><fA11 i1="02" i2="1"><s1>WRIGHT (P. J.)</s1>
</fA11><fA11 i1="03" i2="1"><s1>WANG (L.-F.)</s1>
</fA11><fA11 i1="04" i2="1"><s1>SERGEYEV (O.)</s1>
</fA11><fA11 i1="05" i2="1"><s1>MICHALSKI (W. P.)</s1>
</fA11><fA11 i1="06" i2="1"><s1>BOSSART (K. N.)</s1>
</fA11><fA11 i1="07" i2="1"><s1>BRODER (C. C.)</s1>
</fA11><fA12 i1="01" i2="1"><s1>CALISHER (Charles H.)</s1>
<s9>ed.</s9>
</fA12><fA12 i1="02" i2="1"><s1>GRIFFIN (Diane E.)</s1>
<s9>ed.</s9>
</fA12><fA14 i1="01"><s1>Australian Animal Health Laboratory, CSIRO Livestock Industries</s1>
<s2>Geelong</s2>
<s3>AUS</s3>
<sZ>1 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
</fA14><fA14 i1="02"><s1>Department of Microbiology, Monash University</s1>
<s2>Clayton</s2>
<s3>AUS</s3>
<sZ>2 aut.</sZ>
</fA14><fA14 i1="03"><s1>Department of Microbiology, Uniformed Services University</s1>
<s2>Bethesda, Maryland</s2>
<s3>USA</s3>
<sZ>6 aut.</sZ>
<sZ>7 aut.</sZ>
</fA14><fA18 i1="01" i2="1"><s1>Mérieux Foundation</s1>
<s2>Lyon</s2>
<s3>FRA</s3>
<s9>patr.</s9>
</fA18><fA20><s1>123-131</s1>
</fA20><fA21><s1>2004</s1>
</fA21><fA23 i1="01"><s0>ENG</s0>
</fA23><fA43 i1="01"><s1>INIST</s1>
<s2>6355S</s2>
<s5>354000117181120100</s5>
</fA43><fA44><s0>0000</s0>
<s1>© 2004 INIST-CNRS. All rights reserved.</s1>
</fA44><fA45><s0>32 ref.</s0>
</fA45><fA47 i1="01" i2="1"><s0>04-0472244</s0>
</fA47><fA60><s1>P</s1>
<s2>C</s2>
</fA60><fA64 i1="01" i2="1"><s0>Archives of virology. Supplementum</s0>
</fA64><fA66 i1="01"><s0>AUT</s0>
</fA66><fC01 i1="01" l="ENG"><s0>Hendra virus (HENV) and Nipah virus (NIPV) are classified in the new genus Henipavirus, within the subfamily Paramyxovirinae, family Paramyxoviridae. The genetic and biological characteristics that differentiate henipaviruses from other members of the subfamily are summarized. Although they do not display neuraminidase and hemagglutination activities and in that regard resemble viruses in the genus Morbillivirus, several recent observations highlight similarities between henipaviruses and respiroviruses (genus Respirovirus) in structure and replication strategy. First, three-dimensional modeling studies suggest that the external globular head domain of the HENV G protein resembles that of respiroviruses rather than morbilliviruses. Second, the pattern of transcriptional attenuation in HENV-infected cells resembles that observed with Sendai virus, a respirovirus, and differs from that found in cells infected with measles virus, a morbillivirus. Henipaviruses have a broad host range in vitro and in vivo, indicating wide distribution of cellular receptor molecules. The extensive host range has been confirmed in a quantitative in vitro cell-fusion assay using recombinant vaccinia viruses expressing the attachment and fusion proteins of HENV and NIPV. Cell lines of diverse origin and which are permissive in the in vitro cell fusion assay have been identified and the pattern of relative susceptibilities is the same for both HENV and NIPV, implying that both viruses use the same cell receptor. Protease treatment of permissive cells destroys their ability to fuse with cells expressing viral envelope glycoproteins. Virus overlay protein binding assay (VOPBA) and radio-immune precipitation assays confirm that both HENV and NIPV bind to membrane proteins in the 35-50 kD range. Treatment of cell membrane proteins with N-glycosidase eliminates HeV binding activity in VOPBA whereas treatment with neuraminidase has no effect on binding. Thus preliminary evidence suggests that NIPV and HENV bind to the same glycoprotein receptor via a non-sialic acid-dependant mechanism.</s0>
</fC01><fC02 i1="01" i2="X"><s0>002A05C05</s0>
</fC02><fC03 i1="01" i2="X" l="FRE"><s0>Paramyxoviridae</s0>
<s2>NW</s2>
<s5>01</s5>
</fC03><fC03 i1="01" i2="X" l="ENG"><s0>Paramyxoviridae</s0>
<s2>NW</s2>
<s5>01</s5>
</fC03><fC03 i1="01" i2="X" l="SPA"><s0>Paramyxoviridae</s0>
<s2>NW</s2>
<s5>01</s5>
</fC03><fC03 i1="02" i2="X" l="FRE"><s0>Régulation</s0>
<s5>05</s5>
</fC03><fC03 i1="02" i2="X" l="ENG"><s0>Regulation(control)</s0>
<s5>05</s5>
</fC03><fC03 i1="02" i2="X" l="SPA"><s0>Regulación</s0>
<s5>05</s5>
</fC03><fC03 i1="03" i2="X" l="FRE"><s0>Transcription</s0>
<s5>06</s5>
</fC03><fC03 i1="03" i2="X" l="ENG"><s0>Transcription</s0>
<s5>06</s5>
</fC03><fC03 i1="03" i2="X" l="SPA"><s0>Transcripción</s0>
<s5>06</s5>
</fC03><fC03 i1="04" i2="X" l="FRE"><s0>Protéine</s0>
<s5>07</s5>
</fC03><fC03 i1="04" i2="X" l="ENG"><s0>Protein</s0>
<s5>07</s5>
</fC03><fC03 i1="04" i2="X" l="SPA"><s0>Proteína</s0>
<s5>07</s5>
</fC03><fC03 i1="05" i2="X" l="FRE"><s0>Maladie émergente</s0>
<s2>NM</s2>
<s5>14</s5>
</fC03><fC03 i1="05" i2="X" l="ENG"><s0>Emerging disease</s0>
<s2>NM</s2>
<s5>14</s5>
</fC03><fC03 i1="05" i2="X" l="SPA"><s0>Enfermedad emergente</s0>
<s2>NM</s2>
<s5>14</s5>
</fC03><fC03 i1="06" i2="X" l="FRE"><s0>Virus Nipah</s0>
<s4>INC</s4>
<s5>15</s5>
</fC03><fC03 i1="07" i2="X" l="FRE"><s0>Virus Hendra</s0>
<s4>INC</s4>
<s5>79</s5>
</fC03><fC07 i1="01" i2="X" l="FRE"><s0>Mononegavirales</s0>
<s2>NW</s2>
</fC07><fC07 i1="01" i2="X" l="ENG"><s0>Mononegavirales</s0>
<s2>NW</s2>
</fC07><fC07 i1="01" i2="X" l="SPA"><s0>Mononegavirales</s0>
<s2>NW</s2>
</fC07><fC07 i1="02" i2="X" l="FRE"><s0>Virus</s0>
<s2>NW</s2>
</fC07><fC07 i1="02" i2="X" l="ENG"><s0>Virus</s0>
<s2>NW</s2>
</fC07><fC07 i1="02" i2="X" l="SPA"><s0>Virus</s0>
<s2>NW</s2>
</fC07><fN21><s1>264</s1>
</fN21><pR><fA30 i1="01" i2="1" l="ENG"><s1>Emergence and control of zoonotic viral encephalitis. Symposium</s1>
<s3>Veyrier du Lac FRA</s3>
<s4>2003-04-06</s4>
</fA30>
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