Identification of the Functional Domain of HPIV3 Matrix Protein Interacting with Nucleocapsid Protein
Human parainfluenza virus type 3 (HPIV3) is the main pathogen that causes respiratory infections in infants, young children, and the elderly. Currently, there are no vaccines and effective anti-infective drugs. Studying the replication and proliferation mechanism of HPIV3 is helpful for exploring th...
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doaj-3fdc6996ac6d4e189b0b89c778b4141d2020-12-21T11:41:25ZengHindawi LimitedBioMed Research International2314-61332314-61412020-01-01202010.1155/2020/26161722616172Identification of the Functional Domain of HPIV3 Matrix Protein Interacting with Nucleocapsid ProteinXichuan Deng0Chaoliang Zhang1Kehan Zhang2Nan Lu3Yonglin He4Jia Liu5Zhibang Yang6Guangyuan Zhang7Pathogen Biology and Immunology Laboratory, Tissue and Cell Biology Laboratory, Experimental Teaching Management Center, Chongqing Medical University, Chongqing 401331, ChinaThe First Clinical College of Chongqing Medical University, Chongqing 401331, ChinaThe First Clinical College of Chongqing Medical University, Chongqing 401331, ChinaDepartment of Pathogen Biology, Basic Medical College of Chongqing Medical University, Chongqing 401331, ChinaDepartment of Pathogen Biology, Basic Medical College of Chongqing Medical University, Chongqing 401331, ChinaPathogen Biology and Immunology Laboratory, Tissue and Cell Biology Laboratory, Experimental Teaching Management Center, Chongqing Medical University, Chongqing 401331, ChinaPathogen Biology and Immunology Laboratory, Tissue and Cell Biology Laboratory, Experimental Teaching Management Center, Chongqing Medical University, Chongqing 401331, ChinaPathogen Biology and Immunology Laboratory, Tissue and Cell Biology Laboratory, Experimental Teaching Management Center, Chongqing Medical University, Chongqing 401331, ChinaHuman parainfluenza virus type 3 (HPIV3) is the main pathogen that causes respiratory infections in infants, young children, and the elderly. Currently, there are no vaccines and effective anti-infective drugs. Studying the replication and proliferation mechanism of HPIV3 is helpful for exploring the targets of anti-HPIV3 infection. Matrix protein (M) and nucleocapsid protein (N) are two key structural proteins of HPIV3 that exert important functions in HPIV3 proliferation. Herein, we aim to clarify the functional domains of M and N interaction. HPIV3 M and N expression plasmids of pCAGGS-HA-M and pCAGGS-N-Myc/Flag, M C-terminal truncation mutant plasmids of pCAGGSHA-MΔC120, MΔC170, MΔC190, and MΔC210, and M C-terminal plasmid of pCAGGS-HA-MC190 and C-terminal deletion mutant plasmid of pCAGGS-MΔN143-182 were constructed. By using immunoprecipitation, immunofluorescence, and virus-like particle (VLP) germination experiments, we found that N was encapsulated into M-mediated VLP through N and M interaction. Moreover, the C-terminus of the M played a key role in the interaction between M and N. The C-terminus of the M encapsulated the N into the VLP. We finally determined that the 143-182 amino acids in the M were the functional regions that encapsulated the N into the M-mediated VLP. Our findings confirmed the interaction between M and N and for the first time clarified that the 143-182 amino acid region in M was the functional region that interacted with N, which provides a molecular basis for exploring effective anti-HPIV3 targets.http://dx.doi.org/10.1155/2020/2616172 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Xichuan Deng Chaoliang Zhang Kehan Zhang Nan Lu Yonglin He Jia Liu Zhibang Yang Guangyuan Zhang |
spellingShingle |
Xichuan Deng Chaoliang Zhang Kehan Zhang Nan Lu Yonglin He Jia Liu Zhibang Yang Guangyuan Zhang Identification of the Functional Domain of HPIV3 Matrix Protein Interacting with Nucleocapsid Protein BioMed Research International |
author_facet |
Xichuan Deng Chaoliang Zhang Kehan Zhang Nan Lu Yonglin He Jia Liu Zhibang Yang Guangyuan Zhang |
author_sort |
Xichuan Deng |
title |
Identification of the Functional Domain of HPIV3 Matrix Protein Interacting with Nucleocapsid Protein |
title_short |
Identification of the Functional Domain of HPIV3 Matrix Protein Interacting with Nucleocapsid Protein |
title_full |
Identification of the Functional Domain of HPIV3 Matrix Protein Interacting with Nucleocapsid Protein |
title_fullStr |
Identification of the Functional Domain of HPIV3 Matrix Protein Interacting with Nucleocapsid Protein |
title_full_unstemmed |
Identification of the Functional Domain of HPIV3 Matrix Protein Interacting with Nucleocapsid Protein |
title_sort |
identification of the functional domain of hpiv3 matrix protein interacting with nucleocapsid protein |
publisher |
Hindawi Limited |
series |
BioMed Research International |
issn |
2314-6133 2314-6141 |
publishDate |
2020-01-01 |
description |
Human parainfluenza virus type 3 (HPIV3) is the main pathogen that causes respiratory infections in infants, young children, and the elderly. Currently, there are no vaccines and effective anti-infective drugs. Studying the replication and proliferation mechanism of HPIV3 is helpful for exploring the targets of anti-HPIV3 infection. Matrix protein (M) and nucleocapsid protein (N) are two key structural proteins of HPIV3 that exert important functions in HPIV3 proliferation. Herein, we aim to clarify the functional domains of M and N interaction. HPIV3 M and N expression plasmids of pCAGGS-HA-M and pCAGGS-N-Myc/Flag, M C-terminal truncation mutant plasmids of pCAGGSHA-MΔC120, MΔC170, MΔC190, and MΔC210, and M C-terminal plasmid of pCAGGS-HA-MC190 and C-terminal deletion mutant plasmid of pCAGGS-MΔN143-182 were constructed. By using immunoprecipitation, immunofluorescence, and virus-like particle (VLP) germination experiments, we found that N was encapsulated into M-mediated VLP through N and M interaction. Moreover, the C-terminus of the M played a key role in the interaction between M and N. The C-terminus of the M encapsulated the N into the VLP. We finally determined that the 143-182 amino acids in the M were the functional regions that encapsulated the N into the M-mediated VLP. Our findings confirmed the interaction between M and N and for the first time clarified that the 143-182 amino acid region in M was the functional region that interacted with N, which provides a molecular basis for exploring effective anti-HPIV3 targets. |
url |
http://dx.doi.org/10.1155/2020/2616172 |
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