User:Victoria Fisk/Canine Parvovirus
From Proteopedia
m   | 
			|||
| Line 1: | Line 1: | ||
| - | |||
==History==  | ==History==  | ||
Canine parvovirus, otherwise known as "parvo" is caused by the canine parvovirus type 2 virus. CPV was first discovered in European dogs in 1976. Over the course of two years, it had caused a widespread gastroenteritis epidemic in dogs, predominantly affecting puppies (Cornell). Parvovirus not only affects dogs but also wild animals including raccoons, skunks and foxes. It is currently believed that CPV mutated from Feline Panleukipenia virus through several genetic mutations. CPV2 has a high rate of evolution due to it's increased rate of nucleotide substitution, as shown in RNA virus like the Influenzavirus.  | Canine parvovirus, otherwise known as "parvo" is caused by the canine parvovirus type 2 virus. CPV was first discovered in European dogs in 1976. Over the course of two years, it had caused a widespread gastroenteritis epidemic in dogs, predominantly affecting puppies (Cornell). Parvovirus not only affects dogs but also wild animals including raccoons, skunks and foxes. It is currently believed that CPV mutated from Feline Panleukipenia virus through several genetic mutations. CPV2 has a high rate of evolution due to it's increased rate of nucleotide substitution, as shown in RNA virus like the Influenzavirus.  | ||
| Line 16: | Line 15: | ||
== Structural highlights ==  | == Structural highlights ==  | ||
| - | CPV is a relatively small icosahedral capsid structure measuring 20 to 26 nm in diameter. It contains a major capsid protein, known as VP2. VP1 is a minor structural protein that is present with a specific N-terminal peptide inside the capsid. Each capsid subunit is formed from an eight-stranded<scene name='93/933985/Assymetric_unit/6'>antiparallel β-barrel motif</scene> This motif is a common motif found in many viruses. The CPV surface is made up of loops that connect the β strands. Each icosahedral 2-fold axis contains "spikes" that recognize receptivity and antigenicity of the host. The entire genome is about 5000 nucleotides long.  | + | CPV is a relatively small icosahedral capsid structure measuring 20 to 26 nm in diameter. It contains a major capsid protein, known as VP2. VP1 is a minor structural protein that is present with a specific N-terminal peptide inside the capsid. Each capsid subunit is formed from an eight-stranded <scene name='93/933985/Assymetric_unit/6'>antiparallel β-barrel motif</scene> This motif is a common motif found in many viruses. The CPV surface is made up of loops that connect the β strands. Each icosahedral 2-fold axis contains "spikes" that recognize receptivity and antigenicity of the host. The entire genome is about 5000 nucleotides long.  | 
</StructureSection>  | </StructureSection>  | ||
Revision as of 22:05, 13 November 2022
Contents | 
History
Canine parvovirus, otherwise known as "parvo" is caused by the canine parvovirus type 2 virus. CPV was first discovered in European dogs in 1976. Over the course of two years, it had caused a widespread gastroenteritis epidemic in dogs, predominantly affecting puppies (Cornell). Parvovirus not only affects dogs but also wild animals including raccoons, skunks and foxes. It is currently believed that CPV mutated from Feline Panleukipenia virus through several genetic mutations. CPV2 has a high rate of evolution due to it's increased rate of nucleotide substitution, as shown in RNA virus like the Influenzavirus.
Disease
Canine parvovirus (CPV) is a highly contagious viral disease of dogs that most often causes gastrointestinal distress in puppies. . A rare variant of the disease may be seen in very young (neonatal) puppies is myocarditis (an inflammation of the heart muscle).
Diagnosis
CPV is typically diagnosed through detection of the CPV2 virus in feces using ELISA, or enzyme-linked immunosorbent assay. Other methods of detection include electron microscopy or a hemagglutination test. As the disease progresses, the virus becomes less likely to be detected in the feces by ELISA. When it has caused gastroenteritis, diagnoses can be misdiagnosed as coronavirus or other forms of enteritis causing diseases. When CPV has infected the pericardium, diagnoses can be made easier and quicker.
Treatment
CPV has no approved treatment and can quickly progess depending on the age of the canine, and how much treatment is administered. Most cases of CPV are treated using supportive care, preventing dehydration and increasing quality of life. Vaccination is the best prevention for lethal CPV cases and tests should be administered as soon as avaliable. Supportive case includes intravenus fluids, antibiotic injections, and anti-inflammatories.
Relevance
Structural highlights
CPV is a relatively small icosahedral capsid structure measuring 20 to 26 nm in diameter. It contains a major capsid protein, known as VP2. VP1 is a minor structural protein that is present with a specific N-terminal peptide inside the capsid. Each capsid subunit is formed from an eight-stranded This motif is a common motif found in many viruses. The CPV surface is made up of loops that connect the β strands. Each icosahedral 2-fold axis contains "spikes" that recognize receptivity and antigenicity of the host. The entire genome is about 5000 nucleotides long.
</StructureSection>
References
Nandi, S, and Manoj Kumar. “Canine Parvovirus: Current Perspective.” Indian Journal of Virology : an Official Organ of Indian Virological Society, Springer-Verlag, June 2010, https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3550768/. Organtini, Lindsey J, et al. “Near-Atomic Resolution Structure of a Highly Neutralizing Fab Bound to Canine Parvovirus.” Journal of Virology, American Society for Microbiology, 14 Oct. 2016, https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5068525/. Tsao, Jun, et al. “The Three-Dimensional Structure of Canine Parvovirus and Its Functional Implications.” Science, vol. 251, no. 5000, 1991, pp. 1456–1464., https://doi.org/10.1126/science.2006420. Wikoff, W R, et al. “The Structure of a Neutralized Virus: Canine Parvovirus Complexed with Neutralizing Antibody Fragment.” Structure (London, England : 1993), U.S. National Library of Medicine, 15 July 1994, https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4167666/. Wu, Hao, and Michael G. Rossmann. “The Canine Parvovirus Empty Capsid Structure.” Journal of Molecular Biology, Academic Press, 25 May 2002, https://www.sciencedirect.com/science/article/abs/pii/S0022283683715020?via=ihub.
