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Published in: Virology Journal 1/2013

Open Access 01-12-2013 | Research

N-terminal basic amino acid residues of Beet black scorch virus capsid protein play a critical role in virion assembly and systemic movement

Authors: Xiaofeng Zhang, Xiaofei Zhao, Yanjing Zhang, Shaofang Niu, Feng Qu, Yongliang Zhang, Chenggui Han, Jialin Yu, Dawei Li

Published in: Virology Journal | Issue 1/2013

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Abstract

Background

Beet black scorch virus (BBSV) is a small single-stranded, positive-sense RNA plant virus belonging to the genus Necrovirus, family Tombusviridae. Its capsid protein (CP) contains a 13 amino acid long basic region at the N-terminus, rich in arginine and lysine residues, which is thought to interact with viral RNA to initiate virion assembly.

Results

In the current study, a series of BBSV mutants containing amino acid substitutions as well as deletions within the N-terminal region were generated and examined for their effects on viral RNA replication, virion assembly, and long distance spread in protoplasts and whole host plants of BBSV. The RNA-binding activities of the mutated CPs were also evaluated in vitro. These experiments allowed us to identify two key basic amino acid residues in this region that are responsible for initiating virus assembly through RNA-binding. Proper assembly of BBSV particles is in turn needed for efficient viral systemic movement.

Conclusions

We have identified two basic amino acid residues near the N-terminus of the BBSV CP that bind viral RNA with high affinity to initiate virion assembly. We further provide evidence showing that systemic spread of BBSV in infected plants requires intact virions. This study represents the first in-depth investigation of the role of basic amino acid residues within the N-terminus of a necroviral CP.
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Literature
1.
go back to reference Ivanov KI, Mäkinen K: Coat proteins, host factors and plant viral replication. Curr Opin Virol 2012, 2: 712-718. 10.1016/j.coviro.2012.10.001PubMedCrossRef Ivanov KI, Mäkinen K: Coat proteins, host factors and plant viral replication. Curr Opin Virol 2012, 2: 712-718. 10.1016/j.coviro.2012.10.001PubMedCrossRef
2.
go back to reference Schneemann A: The structural and functional role of RNA in icosahedral virus assembly. Annu Rev Microbiol 2006, 60: 51-67. 10.1146/annurev.micro.60.080805.142304PubMedCrossRef Schneemann A: The structural and functional role of RNA in icosahedral virus assembly. Annu Rev Microbiol 2006, 60: 51-67. 10.1146/annurev.micro.60.080805.142304PubMedCrossRef
3.
go back to reference Choi YG, Grantham GL, Rao ALN: Molecular studies on bromovirus capsid protein: VI. Contributions of the N-terminal arginine-rich motif of BMV capsid protein to virion stability and RNA packaging. Virology 2000, 270: 377-385. 10.1006/viro.2000.0312PubMedCrossRef Choi YG, Grantham GL, Rao ALN: Molecular studies on bromovirus capsid protein: VI. Contributions of the N-terminal arginine-rich motif of BMV capsid protein to virion stability and RNA packaging. Virology 2000, 270: 377-385. 10.1006/viro.2000.0312PubMedCrossRef
4.
go back to reference Choi YG, Rao ALN: Molecular studies on bromovirus capsid protein: VII. Selective packaging of BMV RNA4 by specific N-terminal arginine residues. Virology 2000, 275: 207-217. 10.1006/viro.2000.0513PubMedCrossRef Choi YG, Rao ALN: Molecular studies on bromovirus capsid protein: VII. Selective packaging of BMV RNA4 by specific N-terminal arginine residues. Virology 2000, 275: 207-217. 10.1006/viro.2000.0513PubMedCrossRef
5.
go back to reference Bertolotti-Ciarlet A, White LJ, Chen R, Prasad BVV, Estes MK: Structural requirements for the assembly of Norwalk virus-like particles. J Virol 2002, 76: 4044-4055. 10.1128/JVI.76.8.4044-4055.2002PubMedPubMedCentralCrossRef Bertolotti-Ciarlet A, White LJ, Chen R, Prasad BVV, Estes MK: Structural requirements for the assembly of Norwalk virus-like particles. J Virol 2002, 76: 4044-4055. 10.1128/JVI.76.8.4044-4055.2002PubMedPubMedCentralCrossRef
6.
go back to reference Yusibov V, Loesch-Fries LS: Functional significance of three basic N-terminal amino acids of Alfalfa mosaic virus coat protein. Virology 1998, 242: 1-5. 10.1006/viro.1997.8973PubMedCrossRef Yusibov V, Loesch-Fries LS: Functional significance of three basic N-terminal amino acids of Alfalfa mosaic virus coat protein. Virology 1998, 242: 1-5. 10.1006/viro.1997.8973PubMedCrossRef
7.
go back to reference Lee S-K, Hacker DL: In vitro analysis of an RNA binding site within the N-terminal 30 amino acids of the Southern cowpea mosaic virus coat protein. Virology 2001, 286: 317-327. 10.1006/viro.2001.0979PubMedCrossRef Lee S-K, Hacker DL: In vitro analysis of an RNA binding site within the N-terminal 30 amino acids of the Southern cowpea mosaic virus coat protein. Virology 2001, 286: 317-327. 10.1006/viro.2001.0979PubMedCrossRef
8.
go back to reference Marshall D, Schneemann A: Specific packaging of nod viral RNA2 requires the N-terminus of the capsid protein. Virology 2001, 285: 165-175. 10.1006/viro.2001.0951PubMedCrossRef Marshall D, Schneemann A: Specific packaging of nod viral RNA2 requires the N-terminus of the capsid protein. Virology 2001, 285: 165-175. 10.1006/viro.2001.0951PubMedCrossRef
9.
go back to reference Satheshkumar PS, Lokesh GL, Murthy MRN, Savithri HS: The role of arginine-rich motif and β-annulus in the assembly and stability of Sesbania mosaic virus capsids. J Mol Biol 2005, 353: 447-458. 10.1016/j.jmb.2005.08.021PubMedCrossRef Satheshkumar PS, Lokesh GL, Murthy MRN, Savithri HS: The role of arginine-rich motif and β-annulus in the assembly and stability of Sesbania mosaic virus capsids. J Mol Biol 2005, 353: 447-458. 10.1016/j.jmb.2005.08.021PubMedCrossRef
10.
go back to reference Annamalai P, Apte S, Wilkens S, Rao ALN: Deletion of highly conserved arginine-rich RNA binding motif in Cowpea chlorotic mottle virus capsid protein results in virion structural alterations and RNA packaging constraints. J Virol 2005, 79: 3277-3288. 10.1128/JVI.79.6.3277-3288.2005PubMedPubMedCentralCrossRef Annamalai P, Apte S, Wilkens S, Rao ALN: Deletion of highly conserved arginine-rich RNA binding motif in Cowpea chlorotic mottle virus capsid protein results in virion structural alterations and RNA packaging constraints. J Virol 2005, 79: 3277-3288. 10.1128/JVI.79.6.3277-3288.2005PubMedPubMedCentralCrossRef
11.
go back to reference Yi G, Vaughan RC, Yarbrough I, Dharmaiah S, Kao CC: RNA binding by the Brome mosaic virus capsid protein and the regulation of viral RNA accumulation. J Mol Biol 2009, 391: 314-326. 10.1016/j.jmb.2009.05.065PubMedPubMedCentralCrossRef Yi G, Vaughan RC, Yarbrough I, Dharmaiah S, Kao CC: RNA binding by the Brome mosaic virus capsid protein and the regulation of viral RNA accumulation. J Mol Biol 2009, 391: 314-326. 10.1016/j.jmb.2009.05.065PubMedPubMedCentralCrossRef
12.
go back to reference Lan P, Yeh W-B, Tsai C-W, Lin N-S: A unique glycine-rich motif at the N-terminal region of Bamboo mosaic virus coat protein is required for symptom expression. Mol Plant-Microbe Interact 2010, 23: 903-914. 10.1094/MPMI-23-7-0903PubMedCrossRef Lan P, Yeh W-B, Tsai C-W, Lin N-S: A unique glycine-rich motif at the N-terminal region of Bamboo mosaic virus coat protein is required for symptom expression. Mol Plant-Microbe Interact 2010, 23: 903-914. 10.1094/MPMI-23-7-0903PubMedCrossRef
13.
go back to reference Reade R, Kakani K, Rochon DA: A highly basic KGKKGK sequence in the RNA-binding domain of the Cucumber necrosis virus coat protein is associated with encapsidation of full-length CNV RNA during infection. Virology 2010, 403: 181-188. 10.1016/j.virol.2010.03.045PubMedCrossRef Reade R, Kakani K, Rochon DA: A highly basic KGKKGK sequence in the RNA-binding domain of the Cucumber necrosis virus coat protein is associated with encapsidation of full-length CNV RNA during infection. Virology 2010, 403: 181-188. 10.1016/j.virol.2010.03.045PubMedCrossRef
14.
go back to reference Oda Y, Saeki K, Takahashi Y, Maeda T, Naitow H, Tsukihara T, Fukuyama K: Crystal structure of Tobacco necrosis virus at 2.25 Å resolution. J Mol Biol 2000, 300: 153-169. 10.1006/jmbi.2000.3831PubMedCrossRef Oda Y, Saeki K, Takahashi Y, Maeda T, Naitow H, Tsukihara T, Fukuyama K: Crystal structure of Tobacco necrosis virus at 2.25 Å resolution. J Mol Biol 2000, 300: 153-169. 10.1006/jmbi.2000.3831PubMedCrossRef
15.
go back to reference Cardoso JM, Felix MR, Oliveira S, Clara MI: A Tobacco necrosis virus D isolate from Olea europaea L.: viral characterization and coat protein sequence analysis. Arch Virol 2004, 149: 1129-1138. 10.1007/s00705-003-0258-7PubMedCrossRef Cardoso JM, Felix MR, Oliveira S, Clara MI: A Tobacco necrosis virus D isolate from Olea europaea L.: viral characterization and coat protein sequence analysis. Arch Virol 2004, 149: 1129-1138. 10.1007/s00705-003-0258-7PubMedCrossRef
16.
go back to reference Felix MR, Cardoso JM, Oliveira S, Clara MI: Viral properties, primary structure and phylogenetic analysis of the coat protein of an Olive latent virus 1 isolate from Olea europaea L. Virus Res 2005, 108: 195-198. 10.1016/j.virusres.2004.09.007PubMedCrossRef Felix MR, Cardoso JM, Oliveira S, Clara MI: Viral properties, primary structure and phylogenetic analysis of the coat protein of an Olive latent virus 1 isolate from Olea europaea L. Virus Res 2005, 108: 195-198. 10.1016/j.virusres.2004.09.007PubMedCrossRef
17.
go back to reference Li J, Li M, Li C, Gao Y, Li D, Han C, Yu J: Effects on the local symptoms of subgenomic RNAs expressions and their translational products of Tobacco necrosis virus A Chinese isolate. Chin Sci Bull 2008, 53: 1682-1690. 10.1007/s11434-008-0204-x Li J, Li M, Li C, Gao Y, Li D, Han C, Yu J: Effects on the local symptoms of subgenomic RNAs expressions and their translational products of Tobacco necrosis virus A Chinese isolate. Chin Sci Bull 2008, 53: 1682-1690. 10.1007/s11434-008-0204-x
18.
go back to reference Zhang Y, Li JPUH, Jin J, Zhang X, Chen M, Wang B, Han C, Yu J, Li D: Development of Tobacco necrosis virus A as a vector for efficient and stable expression of FMDV VP1 peptides. Plant Biotechnol J 2010, 8: 506-523. 10.1111/j.1467-7652.2010.00500.xPubMedCrossRef Zhang Y, Li JPUH, Jin J, Zhang X, Chen M, Wang B, Han C, Yu J, Li D: Development of Tobacco necrosis virus A as a vector for efficient and stable expression of FMDV VP1 peptides. Plant Biotechnol J 2010, 8: 506-523. 10.1111/j.1467-7652.2010.00500.xPubMedCrossRef
19.
go back to reference Zhang Y, Zhang X, Niu S, Han C, Yu J, Li D: Nuclear localization of Beet black scorch virus capsid protein and its interaction with importin α. Virus Res 2011, 155: 307-315. 10.1016/j.virusres.2010.10.029PubMedCrossRef Zhang Y, Zhang X, Niu S, Han C, Yu J, Li D: Nuclear localization of Beet black scorch virus capsid protein and its interaction with importin α. Virus Res 2011, 155: 307-315. 10.1016/j.virusres.2010.10.029PubMedCrossRef
20.
go back to reference Lee L, Kaplan IB, Ripoll DR, Liang D, Palukaitis P, Gray SM: A surface loop of the Potato leaf roll virus coat protein is involved in virion assembly, systemic movement, and aphid transmission. J Virol 2005, 79: 1207-1214. 10.1128/JVI.79.2.1207-1214.2005PubMedPubMedCentralCrossRef Lee L, Kaplan IB, Ripoll DR, Liang D, Palukaitis P, Gray SM: A surface loop of the Potato leaf roll virus coat protein is involved in virion assembly, systemic movement, and aphid transmission. J Virol 2005, 79: 1207-1214. 10.1128/JVI.79.2.1207-1214.2005PubMedPubMedCentralCrossRef
21.
go back to reference Tenllado F, Bol JF: Genetic dissection of the multiple functions of Alfalfa mosaic virus coat protein in viral RNA replication, encapsidation, and movement. Virology 2000, 268: 29-40. 10.1006/viro.1999.0170PubMedCrossRef Tenllado F, Bol JF: Genetic dissection of the multiple functions of Alfalfa mosaic virus coat protein in viral RNA replication, encapsidation, and movement. Virology 2000, 268: 29-40. 10.1006/viro.1999.0170PubMedCrossRef
22.
go back to reference Vaewhongs AA, Lommel SA: Virion formation is required for the long-distance movement of Red clover necrotic mosaic virus in movement protein transgenic plants. Virology 1995, 212: 607-613. 10.1006/viro.1995.1518PubMedCrossRef Vaewhongs AA, Lommel SA: Virion formation is required for the long-distance movement of Red clover necrotic mosaic virus in movement protein transgenic plants. Virology 1995, 212: 607-613. 10.1006/viro.1995.1518PubMedCrossRef
23.
go back to reference Saito T, Yamanaka K, Okada Y: Long-distance movement and viral assembly of Tobacco mosaic virus mutants. Virology 1990, 176: 329-336. 10.1016/0042-6822(90)90002-9PubMedCrossRef Saito T, Yamanaka K, Okada Y: Long-distance movement and viral assembly of Tobacco mosaic virus mutants. Virology 1990, 176: 329-336. 10.1016/0042-6822(90)90002-9PubMedCrossRef
24.
go back to reference Dolja VV, Haldeman-Cahill R, Montgomery AE, Vandenbosch KA, Carrington JC: Capsid protein determinants involved in cell-to-cell and long distance movement of Tobacco etch potyvirus . Virology 1995, 206: 1007-1016. 10.1006/viro.1995.1023PubMedCrossRef Dolja VV, Haldeman-Cahill R, Montgomery AE, Vandenbosch KA, Carrington JC: Capsid protein determinants involved in cell-to-cell and long distance movement of Tobacco etch potyvirus . Virology 1995, 206: 1007-1016. 10.1006/viro.1995.1023PubMedCrossRef
25.
go back to reference Molnar A, Havelda Z, Dalmay T, Szutorisz H, Burgyan J: Complete nucleotide sequence of Tobacco necrosis virus strain DH and genes required for RNA replication and virus movement. J Gen Virol 1997, 78: 1235-1239.PubMedCrossRef Molnar A, Havelda Z, Dalmay T, Szutorisz H, Burgyan J: Complete nucleotide sequence of Tobacco necrosis virus strain DH and genes required for RNA replication and virus movement. J Gen Virol 1997, 78: 1235-1239.PubMedCrossRef
26.
go back to reference Pantaleo V, Grieco F, Di Franco A, Martelli GP: The role of the C-terminal region of Olive latent virus 1 coat protein in host systemic infection. Arch Virol 2006, 151: 1973-1983. 10.1007/s00705-006-0767-2PubMedCrossRef Pantaleo V, Grieco F, Di Franco A, Martelli GP: The role of the C-terminal region of Olive latent virus 1 coat protein in host systemic infection. Arch Virol 2006, 151: 1973-1983. 10.1007/s00705-006-0767-2PubMedCrossRef
27.
go back to reference Cao Y, Cai Z, Ding Q, Li D, Han C, Yu J, Liu Y: The complete nucleotide sequence of Beet black scorch virus (BBSV), a new member of the genus Necrovirus . Arch Virol 2002, 147: 2431-2435. 10.1007/s00705-002-0896-1PubMedCrossRef Cao Y, Cai Z, Ding Q, Li D, Han C, Yu J, Liu Y: The complete nucleotide sequence of Beet black scorch virus (BBSV), a new member of the genus Necrovirus . Arch Virol 2002, 147: 2431-2435. 10.1007/s00705-002-0896-1PubMedCrossRef
28.
go back to reference Guo L, Cao Y, Li D, Niu S, Cai Z, Han C, Zhai Y, Yu J: Analysis of nucleotide sequences and multimeric forms of a novel satellite RNA associated with Beet black scorch virus . J Virol 2005, 79: 3664-3674. 10.1128/JVI.79.6.3664-3674.2005PubMedPubMedCentralCrossRef Guo L, Cao Y, Li D, Niu S, Cai Z, Han C, Zhai Y, Yu J: Analysis of nucleotide sequences and multimeric forms of a novel satellite RNA associated with Beet black scorch virus . J Virol 2005, 79: 3664-3674. 10.1128/JVI.79.6.3664-3674.2005PubMedPubMedCentralCrossRef
29.
go back to reference Weiland JJ, Larson RL, Freeman TP, Edwards MC: First report of Beet black scorch virus in the United States. Plant Dis 2006, 90: 828-828.CrossRef Weiland JJ, Larson RL, Freeman TP, Edwards MC: First report of Beet black scorch virus in the United States. Plant Dis 2006, 90: 828-828.CrossRef
30.
go back to reference Koenig R, Valizadeh J: Molecular and serological characterization of an Iranian isolate of Beet black scorch virus . Arch Virol 2008, 153: 1397-1400. 10.1007/s00705-008-0121-yPubMedCrossRef Koenig R, Valizadeh J: Molecular and serological characterization of an Iranian isolate of Beet black scorch virus . Arch Virol 2008, 153: 1397-1400. 10.1007/s00705-008-0121-yPubMedCrossRef
31.
go back to reference González-Vázquez M, Ayala J, García-Arenal F, Fraile A: Occurrence of Beet black scorch virus infecting sugar beet in Europe. Plant Dis 2008, 93: 21-24.CrossRef González-Vázquez M, Ayala J, García-Arenal F, Fraile A: Occurrence of Beet black scorch virus infecting sugar beet in Europe. Plant Dis 2008, 93: 21-24.CrossRef
32.
go back to reference Yuan X, Cao Y, Xi D, Guo L, Han C, Li D, Zhai Y, Yu J: Analysis of the subgenomic RNAs and the small open reading frames of Beet black scorch virus . J Gen Virol 2006, 87: 3077-3086. 10.1099/vir.0.81928-0PubMedCrossRef Yuan X, Cao Y, Xi D, Guo L, Han C, Li D, Zhai Y, Yu J: Analysis of the subgenomic RNAs and the small open reading frames of Beet black scorch virus . J Gen Virol 2006, 87: 3077-3086. 10.1099/vir.0.81928-0PubMedCrossRef
33.
go back to reference Wang X, Zhang Y, Xu J, Shi L, Fan H, Han C, Li D, Yu J: The R-rich motif of Beet black scorch virus P7a movement protein is important for the nuclear localization, nucleolar targeting and viral infectivity. Virus Res 2012, 167: 207-218. 10.1016/j.virusres.2012.05.001PubMedCrossRef Wang X, Zhang Y, Xu J, Shi L, Fan H, Han C, Li D, Yu J: The R-rich motif of Beet black scorch virus P7a movement protein is important for the nuclear localization, nucleolar targeting and viral infectivity. Virus Res 2012, 167: 207-218. 10.1016/j.virusres.2012.05.001PubMedCrossRef
34.
go back to reference Cao Y, Yuan X, Wang X, Guo L, Cai Z, Han C, Li D, Yu J: Effect of Beet black scorch virus coat protein on viral pathogenicity. Prog Biochem Biophys 2006, 33: 127-134. Cao Y, Yuan X, Wang X, Guo L, Cai Z, Han C, Li D, Yu J: Effect of Beet black scorch virus coat protein on viral pathogenicity. Prog Biochem Biophys 2006, 33: 127-134.
35.
go back to reference Fukuyama K, Hirota S, Tsukihara T: Crystallization and preliminary X-ray diffraction studies of Tobacco necrosis virus . J Mol Biol 1987, 196: 961-962. 10.1016/0022-2836(87)90421-9PubMedCrossRef Fukuyama K, Hirota S, Tsukihara T: Crystallization and preliminary X-ray diffraction studies of Tobacco necrosis virus . J Mol Biol 1987, 196: 961-962. 10.1016/0022-2836(87)90421-9PubMedCrossRef
36.
go back to reference Sit TL, Haikal PR, Callaway AS, Lommel SA: A single amino acid mutation in the Carnation ring spot virus capsid protein allows virion formation but prevents systemic infection. J Virol 2001, 75: 9538-9542. 10.1128/JVI.75.19.9538-9542.2001PubMedPubMedCentralCrossRef Sit TL, Haikal PR, Callaway AS, Lommel SA: A single amino acid mutation in the Carnation ring spot virus capsid protein allows virion formation but prevents systemic infection. J Virol 2001, 75: 9538-9542. 10.1128/JVI.75.19.9538-9542.2001PubMedPubMedCentralCrossRef
37.
go back to reference Soto MJ, Chen L-F, Seo Y-S, Gilbertson RL: Identification of regions of the Beet mild curly top virus (family Geminiviridae ) capsid protein involved in systemic infection, virion formation and leafhopper transmission. Virology 2005, 341: 257-270. 10.1016/j.virol.2005.07.009PubMedCrossRef Soto MJ, Chen L-F, Seo Y-S, Gilbertson RL: Identification of regions of the Beet mild curly top virus (family Geminiviridae ) capsid protein involved in systemic infection, virion formation and leafhopper transmission. Virology 2005, 341: 257-270. 10.1016/j.virol.2005.07.009PubMedCrossRef
38.
go back to reference Schmitz I, Rao AL: Deletions in the conserved amino-terminal basic arm of Cucumber mosaic virus coat protein disrupt virion assembly but do not abolish infectivity and cell-to-cell movement. Virology 1998, 248: 323-331. 10.1006/viro.1998.9257PubMedCrossRef Schmitz I, Rao AL: Deletions in the conserved amino-terminal basic arm of Cucumber mosaic virus coat protein disrupt virion assembly but do not abolish infectivity and cell-to-cell movement. Virology 1998, 248: 323-331. 10.1006/viro.1998.9257PubMedCrossRef
39.
go back to reference Nagy JI, Maliga P: Callus induction and plant regeneration from mesophyll protoplasts of Nicotiana sylvestris . Z Pflanzenphysiol 1976, 78: 453-455.CrossRef Nagy JI, Maliga P: Callus induction and plant regeneration from mesophyll protoplasts of Nicotiana sylvestris . Z Pflanzenphysiol 1976, 78: 453-455.CrossRef
40.
go back to reference Kaplan IB, Lee L, Ripoll DR, Palukaitis P, Gildow F, Gray SM: Point mutations in the Potato leaf roll virus major capsid protein alter virion stability and aphid transmission. J Gen Virol 2007, 88: 1821-1830. 10.1099/vir.0.82837-0PubMedCrossRef Kaplan IB, Lee L, Ripoll DR, Palukaitis P, Gildow F, Gray SM: Point mutations in the Potato leaf roll virus major capsid protein alter virion stability and aphid transmission. J Gen Virol 2007, 88: 1821-1830. 10.1099/vir.0.82837-0PubMedCrossRef
41.
go back to reference Rodriguez PLLC: Non-radioactive North-western analysis using biotinylated riboprobes. Biotechniques 1994, 17: 702-706.PubMed Rodriguez PLLC: Non-radioactive North-western analysis using biotinylated riboprobes. Biotechniques 1994, 17: 702-706.PubMed
Metadata
Title
N-terminal basic amino acid residues of Beet black scorch virus capsid protein play a critical role in virion assembly and systemic movement
Authors
Xiaofeng Zhang
Xiaofei Zhao
Yanjing Zhang
Shaofang Niu
Feng Qu
Yongliang Zhang
Chenggui Han
Jialin Yu
Dawei Li
Publication date
01-12-2013
Publisher
BioMed Central
Published in
Virology Journal / Issue 1/2013
Electronic ISSN: 1743-422X
DOI
https://doi.org/10.1186/1743-422X-10-200

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