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Thermal aggregation of SARS-CoV membrane protein

Identifieur interne : 000597 ( PascalFrancis/Corpus ); précédent : 000596; suivant : 000598

Thermal aggregation of SARS-CoV membrane protein

Auteurs : Yi-Nung Lee ; Li-Kuang Chen ; Hsin-Chieh Ma ; Hui-Hua Yang ; Hsin-Pai Li ; Shih-Yen Lo

Source :

RBID : Pascal:05-0443903

Descripteurs français

English descriptors

Abstract

SARS-CoV membrane protein could be detected easily using Western blotting in non-denaturing condition but not regular denaturing treatment. Boiling treatment, causing the aggregation of SARS-CoV membrane protein in the stacking gels, results in the failure to detect the membrane protein in the separating gels. Aggregated membrane proteins could not be dissociated by 1% Triton-X 100, 6 M urea, or 2% SDS. The region with amino acid residues from 51 to 170 is responsible for thermal aggregation of SARS-CoV membrane protein. Hydrophobic regions with amino acid residues from 61 to 90, from 91 to 100, from 136 to 170, are essential for this protein aggregation. Thermal aggregation of SARS-CoV membrane protein is not unique among structural proteins of coronaviruses. However, SARS-CoV membrane protein seems to be more sensitive to heat treatment, since the membrane protein of MHV-JHM, another member of the Coronaviridae, would not aggregate after the same treatment. Therefore, if SARS-CoV membrane protein needs to be analyzed using SDS-PAGE, boiling should be avoided. Thermal aggregation of SARS-CoV membrane protein may be one of the reasons for the inactivation of this virus by heat. The unusual property of SARS-CoV membrane protein aggregation induced by heat also provides a model for the study of protein aggregation.

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

pA  
A01 01  1    @0 0166-0934
A02 01      @0 JVMEDH
A03   1    @0 J. virol. methods
A05       @2 129
A06       @2 2
A08 01  1  ENG  @1 Thermal aggregation of SARS-CoV membrane protein
A11 01  1    @1 LEE (Yi-Nung)
A11 02  1    @1 CHEN (Li-Kuang)
A11 03  1    @1 MA (Hsin-Chieh)
A11 04  1    @1 YANG (Hui-Hua)
A11 05  1    @1 LI (Hsin-Pai)
A11 06  1    @1 LO (Shih-Yen)
A14 01      @1 Graduate Institute of Molecular and Cellular Biology, Tzu Chi University @2 Hualien @3 TWN @Z 1 aut. @Z 6 aut.
A14 02      @1 Graduate Institute of Medical Sciences, Tzu Chi University @2 Hualien @3 TWN @Z 2 aut. @Z 3 aut. @Z 4 aut. @Z 6 aut.
A14 03      @1 Department of Emergency Medicine, Buddhist Till Chi General Hospital @2 Hualien @3 TWN @Z 2 aut.
A14 04      @1 Graduate Institute of Basic Medical Sciences, Chang Gang University @2 Taoyuan @3 TWN @Z 5 aut.
A14 05      @1 Department of Laboratory Medicine and Biotechnology, Tzu Chi University, College of Medicine, 701 Section 3, Chung Yang Road @2 Hualien 970 @3 TWN @Z 6 aut.
A20       @1 152-161
A21       @1 2005
A23 01      @0 ENG
A43 01      @1 INIST @2 18295 @5 354000135561140060
A44       @0 0000 @1 © 2005 INIST-CNRS. All rights reserved.
A45       @0 32 ref.
A47 01  1    @0 05-0443903
A60       @1 P
A61       @0 A
A64 01  1    @0 Journal of virological methods
A66 01      @0 NLD
C01 01    ENG  @0 SARS-CoV membrane protein could be detected easily using Western blotting in non-denaturing condition but not regular denaturing treatment. Boiling treatment, causing the aggregation of SARS-CoV membrane protein in the stacking gels, results in the failure to detect the membrane protein in the separating gels. Aggregated membrane proteins could not be dissociated by 1% Triton-X 100, 6 M urea, or 2% SDS. The region with amino acid residues from 51 to 170 is responsible for thermal aggregation of SARS-CoV membrane protein. Hydrophobic regions with amino acid residues from 61 to 90, from 91 to 100, from 136 to 170, are essential for this protein aggregation. Thermal aggregation of SARS-CoV membrane protein is not unique among structural proteins of coronaviruses. However, SARS-CoV membrane protein seems to be more sensitive to heat treatment, since the membrane protein of MHV-JHM, another member of the Coronaviridae, would not aggregate after the same treatment. Therefore, if SARS-CoV membrane protein needs to be analyzed using SDS-PAGE, boiling should be avoided. Thermal aggregation of SARS-CoV membrane protein may be one of the reasons for the inactivation of this virus by heat. The unusual property of SARS-CoV membrane protein aggregation induced by heat also provides a model for the study of protein aggregation.
C02 01  X    @0 002A05C09
C03 01  X  FRE  @0 Agrégation @5 05
C03 01  X  ENG  @0 Aggregation @5 05
C03 01  X  SPA  @0 Agregación @5 05
C03 02  X  FRE  @0 Protéine membranaire @5 06
C03 02  X  ENG  @0 Membrane protein @5 06
C03 02  X  SPA  @0 Proteína membranar @5 06
C03 03  X  FRE  @0 Microbiologie @5 07
C03 03  X  ENG  @0 Microbiology @5 07
C03 03  X  SPA  @0 Microbiología @5 07
C03 04  X  FRE  @0 Méthode @5 08
C03 04  X  ENG  @0 Method @5 08
C03 04  X  SPA  @0 Método @5 08
C03 05  X  FRE  @0 Virologie @5 09
C03 05  X  ENG  @0 Virology @5 09
C03 05  X  SPA  @0 Virología @5 09
C03 06  X  FRE  @0 Syndrome respiratoire aigu sévère @2 NM @5 14
C03 06  X  ENG  @0 Severe acute respiratory syndrome @2 NM @5 14
C03 06  X  SPA  @0 Síndrome respiratorio agudo severo @2 NM @5 14
C07 01  X  FRE  @0 Virose
C07 01  X  ENG  @0 Viral disease
C07 01  X  SPA  @0 Virosis
C07 02  X  FRE  @0 Infection
C07 02  X  ENG  @0 Infection
C07 02  X  SPA  @0 Infección
N21       @1 311
N44 01      @1 OTO
N82       @1 OTO

Format Inist (serveur)

NO : PASCAL 05-0443903 INIST
ET : Thermal aggregation of SARS-CoV membrane protein
AU : LEE (Yi-Nung); CHEN (Li-Kuang); MA (Hsin-Chieh); YANG (Hui-Hua); LI (Hsin-Pai); LO (Shih-Yen)
AF : Graduate Institute of Molecular and Cellular Biology, Tzu Chi University/Hualien/Taïwan (1 aut., 6 aut.); Graduate Institute of Medical Sciences, Tzu Chi University/Hualien/Taïwan (2 aut., 3 aut., 4 aut., 6 aut.); Department of Emergency Medicine, Buddhist Till Chi General Hospital/Hualien/Taïwan (2 aut.); Graduate Institute of Basic Medical Sciences, Chang Gang University/Taoyuan/Taïwan (5 aut.); Department of Laboratory Medicine and Biotechnology, Tzu Chi University, College of Medicine, 701 Section 3, Chung Yang Road/Hualien 970/Taïwan (6 aut.)
DT : Publication en série; Niveau analytique
SO : Journal of virological methods; ISSN 0166-0934; Coden JVMEDH; Pays-Bas; Da. 2005; Vol. 129; No. 2; Pp. 152-161; Bibl. 32 ref.
LA : Anglais
EA : SARS-CoV membrane protein could be detected easily using Western blotting in non-denaturing condition but not regular denaturing treatment. Boiling treatment, causing the aggregation of SARS-CoV membrane protein in the stacking gels, results in the failure to detect the membrane protein in the separating gels. Aggregated membrane proteins could not be dissociated by 1% Triton-X 100, 6 M urea, or 2% SDS. The region with amino acid residues from 51 to 170 is responsible for thermal aggregation of SARS-CoV membrane protein. Hydrophobic regions with amino acid residues from 61 to 90, from 91 to 100, from 136 to 170, are essential for this protein aggregation. Thermal aggregation of SARS-CoV membrane protein is not unique among structural proteins of coronaviruses. However, SARS-CoV membrane protein seems to be more sensitive to heat treatment, since the membrane protein of MHV-JHM, another member of the Coronaviridae, would not aggregate after the same treatment. Therefore, if SARS-CoV membrane protein needs to be analyzed using SDS-PAGE, boiling should be avoided. Thermal aggregation of SARS-CoV membrane protein may be one of the reasons for the inactivation of this virus by heat. The unusual property of SARS-CoV membrane protein aggregation induced by heat also provides a model for the study of protein aggregation.
CC : 002A05C09
FD : Agrégation; Protéine membranaire; Microbiologie; Méthode; Virologie; Syndrome respiratoire aigu sévère
FG : Virose; Infection
ED : Aggregation; Membrane protein; Microbiology; Method; Virology; Severe acute respiratory syndrome
EG : Viral disease; Infection
SD : Agregación; Proteína membranar; Microbiología; Método; Virología; Síndrome respiratorio agudo severo
LO : INIST-18295.354000135561140060
ID : 05-0443903

Links to Exploration step

Pascal:05-0443903

Le document en format XML

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<div type="abstract" xml:lang="en">SARS-CoV membrane protein could be detected easily using Western blotting in non-denaturing condition but not regular denaturing treatment. Boiling treatment, causing the aggregation of SARS-CoV membrane protein in the stacking gels, results in the failure to detect the membrane protein in the separating gels. Aggregated membrane proteins could not be dissociated by 1% Triton-X 100, 6 M urea, or 2% SDS. The region with amino acid residues from 51 to 170 is responsible for thermal aggregation of SARS-CoV membrane protein. Hydrophobic regions with amino acid residues from 61 to 90, from 91 to 100, from 136 to 170, are essential for this protein aggregation. Thermal aggregation of SARS-CoV membrane protein is not unique among structural proteins of coronaviruses. However, SARS-CoV membrane protein seems to be more sensitive to heat treatment, since the membrane protein of MHV-JHM, another member of the Coronaviridae, would not aggregate after the same treatment. Therefore, if SARS-CoV membrane protein needs to be analyzed using SDS-PAGE, boiling should be avoided. Thermal aggregation of SARS-CoV membrane protein may be one of the reasons for the inactivation of this virus by heat. The unusual property of SARS-CoV membrane protein aggregation induced by heat also provides a model for the study of protein aggregation.</div>
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<fC03 i1="01" i2="X" l="ENG">
<s0>Aggregation</s0>
<s5>05</s5>
</fC03>
<fC03 i1="01" i2="X" l="SPA">
<s0>Agregación</s0>
<s5>05</s5>
</fC03>
<fC03 i1="02" i2="X" l="FRE">
<s0>Protéine membranaire</s0>
<s5>06</s5>
</fC03>
<fC03 i1="02" i2="X" l="ENG">
<s0>Membrane protein</s0>
<s5>06</s5>
</fC03>
<fC03 i1="02" i2="X" l="SPA">
<s0>Proteína membranar</s0>
<s5>06</s5>
</fC03>
<fC03 i1="03" i2="X" l="FRE">
<s0>Microbiologie</s0>
<s5>07</s5>
</fC03>
<fC03 i1="03" i2="X" l="ENG">
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<s5>07</s5>
</fC03>
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<s0>Microbiología</s0>
<s5>07</s5>
</fC03>
<fC03 i1="04" i2="X" l="FRE">
<s0>Méthode</s0>
<s5>08</s5>
</fC03>
<fC03 i1="04" i2="X" l="ENG">
<s0>Method</s0>
<s5>08</s5>
</fC03>
<fC03 i1="04" i2="X" l="SPA">
<s0>Método</s0>
<s5>08</s5>
</fC03>
<fC03 i1="05" i2="X" l="FRE">
<s0>Virologie</s0>
<s5>09</s5>
</fC03>
<fC03 i1="05" i2="X" l="ENG">
<s0>Virology</s0>
<s5>09</s5>
</fC03>
<fC03 i1="05" i2="X" l="SPA">
<s0>Virología</s0>
<s5>09</s5>
</fC03>
<fC03 i1="06" i2="X" l="FRE">
<s0>Syndrome respiratoire aigu sévère</s0>
<s2>NM</s2>
<s5>14</s5>
</fC03>
<fC03 i1="06" i2="X" l="ENG">
<s0>Severe acute respiratory syndrome</s0>
<s2>NM</s2>
<s5>14</s5>
</fC03>
<fC03 i1="06" i2="X" l="SPA">
<s0>Síndrome respiratorio agudo severo</s0>
<s2>NM</s2>
<s5>14</s5>
</fC03>
<fC07 i1="01" i2="X" l="FRE">
<s0>Virose</s0>
</fC07>
<fC07 i1="01" i2="X" l="ENG">
<s0>Viral disease</s0>
</fC07>
<fC07 i1="01" i2="X" l="SPA">
<s0>Virosis</s0>
</fC07>
<fC07 i1="02" i2="X" l="FRE">
<s0>Infection</s0>
</fC07>
<fC07 i1="02" i2="X" l="ENG">
<s0>Infection</s0>
</fC07>
<fC07 i1="02" i2="X" l="SPA">
<s0>Infección</s0>
</fC07>
<fN21>
<s1>311</s1>
</fN21>
<fN44 i1="01">
<s1>OTO</s1>
</fN44>
<fN82>
<s1>OTO</s1>
</fN82>
</pA>
</standard>
<server>
<NO>PASCAL 05-0443903 INIST</NO>
<ET>Thermal aggregation of SARS-CoV membrane protein</ET>
<AU>LEE (Yi-Nung); CHEN (Li-Kuang); MA (Hsin-Chieh); YANG (Hui-Hua); LI (Hsin-Pai); LO (Shih-Yen)</AU>
<AF>Graduate Institute of Molecular and Cellular Biology, Tzu Chi University/Hualien/Taïwan (1 aut., 6 aut.); Graduate Institute of Medical Sciences, Tzu Chi University/Hualien/Taïwan (2 aut., 3 aut., 4 aut., 6 aut.); Department of Emergency Medicine, Buddhist Till Chi General Hospital/Hualien/Taïwan (2 aut.); Graduate Institute of Basic Medical Sciences, Chang Gang University/Taoyuan/Taïwan (5 aut.); Department of Laboratory Medicine and Biotechnology, Tzu Chi University, College of Medicine, 701 Section 3, Chung Yang Road/Hualien 970/Taïwan (6 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>Journal of virological methods; ISSN 0166-0934; Coden JVMEDH; Pays-Bas; Da. 2005; Vol. 129; No. 2; Pp. 152-161; Bibl. 32 ref.</SO>
<LA>Anglais</LA>
<EA>SARS-CoV membrane protein could be detected easily using Western blotting in non-denaturing condition but not regular denaturing treatment. Boiling treatment, causing the aggregation of SARS-CoV membrane protein in the stacking gels, results in the failure to detect the membrane protein in the separating gels. Aggregated membrane proteins could not be dissociated by 1% Triton-X 100, 6 M urea, or 2% SDS. The region with amino acid residues from 51 to 170 is responsible for thermal aggregation of SARS-CoV membrane protein. Hydrophobic regions with amino acid residues from 61 to 90, from 91 to 100, from 136 to 170, are essential for this protein aggregation. Thermal aggregation of SARS-CoV membrane protein is not unique among structural proteins of coronaviruses. However, SARS-CoV membrane protein seems to be more sensitive to heat treatment, since the membrane protein of MHV-JHM, another member of the Coronaviridae, would not aggregate after the same treatment. Therefore, if SARS-CoV membrane protein needs to be analyzed using SDS-PAGE, boiling should be avoided. Thermal aggregation of SARS-CoV membrane protein may be one of the reasons for the inactivation of this virus by heat. The unusual property of SARS-CoV membrane protein aggregation induced by heat also provides a model for the study of protein aggregation.</EA>
<CC>002A05C09</CC>
<FD>Agrégation; Protéine membranaire; Microbiologie; Méthode; Virologie; Syndrome respiratoire aigu sévère</FD>
<FG>Virose; Infection</FG>
<ED>Aggregation; Membrane protein; Microbiology; Method; Virology; Severe acute respiratory syndrome</ED>
<EG>Viral disease; Infection</EG>
<SD>Agregación; Proteína membranar; Microbiología; Método; Virología; Síndrome respiratorio agudo severo</SD>
<LO>INIST-18295.354000135561140060</LO>
<ID>05-0443903</ID>
</server>
</inist>
</record>

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