Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus. The disease is the cause of the 2019–20 coronavirus outbreak (1). SARS-CoV-2 is the seventh member of the enveloped, positive-stranded RNA viruses that are able to infect humans. The SARS-CoV-2 genome, like other coronaviruses, encodes for multiple structural and nonstructural proteins. The structural proteins include spike protein (S), envelope protein (E), membrane glycoprotein (M), nucleocapsid phosphoprotein (N), and the nonstructural proteins include open reading frame 1ab (ORF1ab), ORF3a, ORF6, ORF7a, ORF8, and ORF10 (2).The membrane (M) protein or matrix protein is the most abundant structural protein and defines the shape of the viral envelope (3). It is an integral membrane protein involved in the budding of the viral particles and interacts with S (Spike) protein. It involves in organization of the nucleoprotein inside, which includes many copies of the N (nucleocapsid) protein bound to the genomic RNA. The M protein holds dominant cellular immunogenicity and has been determined as a protective antigen in humoral responses, which suggests it would serve as a potential target in vaccine design (4).

Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus. The disease is the cause of the 2019–20 coronavirus outbreak (1). SARS-CoV-2 is the seventh member of the enveloped, positive-stranded RNA viruses that are able to infect humans. The SARS-CoV-2 genome, like other coronaviruses, encodes for multiple structural and nonstructural proteins. The structural proteins include spike protein (S), envelope protein (E), membrane glycoprotein (M), nucleocapsid phosphoprotein (N), and the nonstructural proteins include open reading frame 1ab (ORF1ab), ORF3a, ORF6, ORF7a, ORF8, and ORF10 (2).The membrane (M) protein or matrix protein is the most abundant structural protein and defines the shape of the viral envelope (3). It is an integral membrane protein involved in the budding of the viral particles and interacts with S (Spike) protein. It involves in organization of the nucleoprotein inside, which includes many copies of the N (nucleocapsid) protein bound to the genomic RNA. The M protein holds dominant cellular immunogenicity and has been determined as a protective antigen in humoral responses, which suggests it would serve as a potential target in vaccine design (4).

Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus (1). The disease is the cause of the 2019–20 coronavirus outbreak (2). The structure of 2019-nCoV consists of the following: a spike protein (S), hemagglutinin-esterease dimer (HE), a membrane glycoprotein (M), an envelope protein (E) a nucleoclapid protein (N) and RNA. NSP8 plays a role in viral RNA synthesis (3,4,5). Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, it may synthesize substantially longer products than oligonucleotide primers (6).

Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus (1). The disease is the cause of the 2019–20 coronavirus outbreak (2). The structure of 2019-nCoV consists of the following: a spike protein (S), hemagglutinin-esterease dimer (HE), a membrane glycoprotein (M), an envelope protein (E) a nucleoclapid protein (N) and RNA. NSP8 plays a role in viral RNA synthesis (3,4,5). Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, it may synthesize substantially longer products than oligonucleotide primers (6).

Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus (1). The disease is the cause of the 2019–20 coronavirus outbreak (2). The structure of 2019-nCoV consists of the following: a spike protein (S), hemagglutinin-esterease dimer (HE), a membrane glycoprotein (M), an envelope protein (E) a nucleoclapid protein (N) and RNA. NSP9 may participate in viral replication by acting as a ssRNA-binding protein (3).

Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus (1). The disease is the cause of the 2019–20 coronavirus outbreak (2). The structure of 2019-nCoV consists of the following: a spike protein (S), hemagglutinin-esterease dimer (HE), a membrane glycoprotein (M), an envelope protein (E) a nucleoclapid protein (N) and RNA. NSP9 may participate in viral replication by acting as a ssRNA-binding protein (3).

Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus (1). The disease is the cause of the 2019–20 coronavirus outbreak (2). The structure of 2019-nCoV consists of the following: a spike protein (S), hemagglutinin-esterease dimer (HE), a membrane glycoprotein (M), an envelope protein (E) a nucleoclapid protein (N) and RNA. NSP9 may participate in viral replication by acting as a ssRNA-binding protein (3).

Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus (1). The disease is the cause of the 2019–20 coronavirus outbreak (2). The structure of 2019-nCoV consists of the following: a spike protein (S), hemagglutinin-esterease dimer (HE), a membrane glycoprotein (M), an envelope protein (E) a nucleoclapid protein (N) and RNA. NSP9 may participate in viral replication by acting as a ssRNA-binding protein (3).

Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus. The disease is the cause of the 2019–20 coronavirus outbreak (1). SARS-CoV-2 is the seventh member of the enveloped, positive-stranded RNA viruses that are able to infect humans. The SARS-CoV-2 genome, like other coronaviruses, encodes for multiple structural and nonstructural proteins. The structural proteins include spike protein (S), envelope protein (E), membrane glycoprotein (M), nucleocapsid phosphoprotein (N), and the nonstructural proteins include open reading frame 1ab (ORF1ab), ORF3a, ORF6, ORF7a, ORF8, and ORF10 (2).The membrane (M) protein or matrix protein is the most abundant structural protein and defines the shape of the viral envelope (3). It is an integral membrane protein involved in the budding of the viral particles and interacts with S (Spike) protein. It involves in organization of the nucleoprotein inside, which includes many copies of the N (nucleocapsid) protein bound to the genomic RNA. The M protein holds dominant cellular immunogenicity and has been determined as a protective antigen in humoral responses, which suggests it would serve as a potential target in vaccine design (4).

Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus. The disease is the cause of the 2019–20 coronavirus outbreak (1). SARS-CoV-2 is the seventh member of the enveloped, positive-stranded RNA viruses that are able to infect humans. The SARS-CoV-2 genome, like other coronaviruses, encodes for multiple structural and nonstructural proteins. The structural proteins include spike protein (S), envelope protein (E), membrane glycoprotein (M), nucleocapsid phosphoprotein (N), and the nonstructural proteins include open reading frame 1ab (ORF1ab), ORF3a, ORF6, ORF7a, ORF8, and ORF10 (2).The membrane (M) protein or matrix protein is the most abundant structural protein and defines the shape of the viral envelope (3). It is an integral membrane protein involved in the budding of the viral particles and interacts with S (Spike) protein. It involves in organization of the nucleoprotein inside, which includes many copies of the N (nucleocapsid) protein bound to the genomic RNA. The M protein holds dominant cellular immunogenicity and has been determined as a protective antigen in humoral responses, which suggests it would serve as a potential target in vaccine design (4).

Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus (1). The disease is the cause of the 2019–20 coronavirus outbreak (2). The structure of 2019-nCoV consists of the following: a spike protein (S), hemagglutinin-esterease dimer (HE), a membrane glycoprotein (M), an envelope protein (E) a nucleoclapid protein (N) and RNA. NSP8 plays a role in viral RNA synthesis (3,4,5). Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, it may synthesize substantially longer products than oligonucleotide primers (6).

Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus (1). The disease is the cause of the 2019–20 coronavirus outbreak (2). The structure of 2019-nCoV consists of the following: a spike protein (S), hemagglutinin-esterease dimer (HE), a membrane glycoprotein (M), an envelope protein (E) a nucleoclapid protein (N) and RNA. NSP8 plays a role in viral RNA synthesis (3,4,5). Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, it may synthesize substantially longer products than oligonucleotide primers (6).

Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus (1). The disease is the cause of the 2019–20 coronavirus outbreak (2). The structure of 2019-nCoV consists of the following: a spike protein (S), hemagglutinin-esterease dimer (HE), a membrane glycoprotein (M), an envelope protein (E) a nucleoclapid protein (N) and RNA. The envelope protein is a small polypeptide that contains at least one α-helical transmembrane domain. It involves in several aspects of the virus's life cycle, such as assembly, budding, envelope formation, and pathogenesis. E protein has membrane permeabilizing activity, which provides a possible rationale to inhibit in vitro ion channel activity of some synthetic corona virus E proteins, and also viral replication (3).

Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus (1). The disease is the cause of the 2019–20 coronavirus outbreak (2). The structure of 2019-nCoV consists of the following: a spike protein (S), hemagglutinin-esterease dimer (HE), a membrane glycoprotein (M), an envelope protein (E) a nucleoclapid protein (N) and RNA. The envelope protein is a small polypeptide that contains at least one α-helical transmembrane domain. It involves in several aspects of the virus's life cycle, such as assembly, budding, envelope formation, and pathogenesis. E protein has membrane permeabilizing activity, which provides a possible rationale to inhibit in vitro ion channel activity of some synthetic corona virus E proteins, and also viral replication (3).

Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus (1). The disease is the cause of the 2019–20 coronavirus outbreak (2). The structure of 2019-nCoV consists of the following: a spike protein (S), hemagglutinin-esterease dimer (HE), a membrane glycoprotein (M), an envelope protein (E) a nucleoclapid protein (N) and RNA. NSP2 may play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses (3).

Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus (1). The disease is the cause of the 2019–20 coronavirus outbreak (2). The structure of 2019-nCoV consists of the following: a spike protein (S), hemagglutinin-esterease dimer (HE), a membrane glycoprotein (M), an envelope protein (E) a nucleoclapid protein (N) and RNA. NSP2 may play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses (3).

Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus (1). The disease is the cause of the 2019–20 coronavirus outbreak (2). The structure of 2019-nCoV consists of the following: a spike protein (S), hemagglutinin-esterease dimer (HE), a membrane glycoprotein (M), an envelope protein (E) a nucleoclapid protein (N) and RNA. NSP2 may play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses (3).