Description: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is an enveloped, positive-sense, single-stranded RNA virus that causes coronavirus disease 2019 (COVID-19). Virus particles include the RNA genetic material and structural proteins needed for invasion of host cells. Once inside the cell the infecting RNA is used to encode structural proteins that make up virus particles, nonstructural proteins that direct virus assembly, transcription, replication and host control and accessory proteins whose function has not been determined.~ ORF1ab, the largest gene, contains overlapping open reading frames that encode polyproteins PP1ab and PP1a. The polyproteins are cleaved to yield 16 nonstructural proteins, NSP1-16. Production of the longer (PP1ab) or shorter protein (PP1a) depends on a -1 ribosomal frameshifting event. The proteins, based on similarity to other coronaviruses, include the papain-like proteinase protein (NSP3), 3C-like proteinase (NSP5), RNA-dependent RNA polymerase (NSP12, RdRp), helicase (NSP13, HEL), endoRNAse (NSP15), 2'-O-Ribose-Methyltransferase (NSP16) and other nonstructural proteins. SARS-CoV-2 nonstructural proteins are responsible for viral transcription, replication, proteolytic processing, suppression of host immune responses and suppression of host gene expression. The RNA-dependent RNA polymerase is a target of antiviral therapies.

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: SARS Envelope Antibody: A novel coronavirus has recently been identified as the causative agent of SARS (Severe Acute Respiratory Syndrome). Coronaviruses are a major cause of upper respiratory diseases in humans. The genomes of these viruses are positive-stranded RNA approximately 27-31kb in length. SARS infection can be mediated by the binding of the viral spike protein, a glycosylated 139 kDa protein and the major surface antigen of the virus, to the angiotensin-converting enzyme 2 (ACE2) on target cells. This binding can be blocked by a soluble form of ACE2.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 coronavirus E proteins, and also viral replication.

Description: SARS Envelope Antibody: A novel coronavirus has recently been identified as the causative agent of SARS (Severe Acute Respiratory Syndrome). Coronaviruses are a major cause of upper respiratory diseases in humans. The genomes of these viruses are positive-stranded RNA approximately 27-31kb in length. SARS infection can be mediated by the binding of the viral spike protein, a glycosylated 139 kDa protein and the major surface antigen of the virus, to the angiotensin-converting enzyme 2 (ACE2) on target cells. This binding can be blocked by a soluble form of ACE2.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 coronavirus E proteins, and also viral replication.

Description: SARS-CoV Spike Antibody: A novel coronavirus has been identified as the causative agent of SARS (Severe Acute Respiratory Syndrome). Coronaviruses are a major cause of upper respiratory diseases in humans. The genomes of these viruses are positive-stranded RNA approximately 27-31kb in length. SARS infection can be mediated by the binding of the viral spike protein, a glycosylated 139 kDa protein and the major surface antigen of the virus, to the angiotensin-converting enzyme 2 (ACE2) on target cells. This binding can be blocked by a soluble form of ACE2.

Description: SARS-CoV Spike Antibody: A novel coronavirus has been identified as the causative agent of SARS (Severe Acute Respiratory Syndrome). Coronaviruses are a major cause of upper respiratory diseases in humans. The genomes of these viruses are positive-stranded RNA approximately 27-31kb in length. SARS infection can be mediated by the binding of the viral spike protein, a glycosylated 139 kDa protein and the major surface antigen of the virus, to the angiotensin-converting enzyme 2 (ACE2) on target cells. This binding can be blocked by a soluble form of ACE2.

Description: SARS-CoV Spike Antibody: A novel coronavirus has recently been identified as the causative agent of SARS (Severe Acute Respiratory Syndrome). Coronaviruses are a major cause of upper respiratory diseases in humans. The genomes of these viruses are positive-stranded RNA approximately 27-31kb in length. SARS infection can be mediated by the binding of the viral spike protein, a glycosylated 139 kDa protein and the major surface antigen of the virus, to the angiotensin-converting enzyme 2 (ACE2) on target cells. This binding can be blocked by a soluble form of ACE2.

Description: SARS-CoV-2 (COVID-19) NSP8 Peptide

Description: SARS-CoV-2 (COVID-19) NSP9 Peptide

Description: SARS-CoV-2 (COVID-19) NSP9 Peptide

Description: SARS-CoV-2 (COVID-19) NSP8 Peptide

Description: SARS-CoV-2 (COVID-19) NSP2 Peptide

Description: SARS-CoV-2 (COVID-19) NSP2 Peptide

Description: SARS-CoV-2 (COVID-19) NSP4 Peptide

Description: SARS-CoV-2 (COVID-19) NSP6 Peptide

Description: SARS-CoV-2 (COVID-19) ORF6 Peptide

Description: SARS-CoV-2 (COVID-19) ORF8 Peptide

Description: SARS-CoV-2 (COVID-19) ORF8 Peptide

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. NSP7 plays a role in viral RNA synthesis (3,4,5). It forms a hexadecamer with nsp8 (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.

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. NSP7 plays a role in viral RNA synthesis (3,4,5). It forms a hexadecamer with nsp8 (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.

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).