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Parainfluenza Virus 2, Human

Parainfluenza Virus 2 is a member of the Paramyxoviridae family, known to cause respiratory infections in humans.
This virus is a common cause of croup, bronchiolitis, and pneumonia, primarily affecting young children.
Parainfluenza Virus 2 is transmited through respiratory droplets and can lead to severe illnesses, especially in immunocompromised individuals.
Understanding the latest research on this virus is crucial for developing effective treatment and prevention strategies.
PubCompare.ai can help optimize your studies by comparing protocols from literature, preprints, and patents, enabling you to identify the most reproducible and accurate methods.
Enhance your research effeciency and accuarcy with PubCompare.ai.

Most cited protocols related to «Parainfluenza Virus 2, Human»

1
Influenza Virus Binding Assay
Viruses were grown in MDCK cells, clarified by low-speed centrifugation, laid over a cushion of 30% sucrose in phosphate-buffered saline (PBS), and ultracentrifuged at 25,000 rpm for 2 h at 4°C. Virus stocks were aliquoted and stored at −80°C. Virus concentrations were determined by using HA assays with 0.5 % (vol/vol) TRBC. The direct receptor-binding capacity of viruses was examined by use of a solid-phase binding assay as previously described9 (link). Microtitre plates (Nunc) were incubated with the sodium salts of sialylglycopolymers [poly-L-glutamic acid backbones containing N-acetylneuraminic acid linked to galactose through either an α2,3 (Neu5Acα2,3Galβ1,4GlcNAcβ1-pAP) or an α2,6 (Neu5Acα2,6Galβ1,4GlcNAcβ1-pAP) bond] in PBS at 4°C overnight. After the glycopolymer solution was removed, the plates were blocked with 0.15 ml of PBS containing 4% bovine serum albumin (BSA) at room temperature for 1 h. Following four successive washes with ice-cold PBS, the plates were incubated in a solution containing influenza virus (8 to 32 HA units in PBS) at 4°C overnight. After washing as described above, the plates were incubated for 2 h at 4°C with rabbit polyclonal antiserum to either human H1N1 or avian H5N1 virus. The plates were then washed again as before and incubated with horseradish peroxidase (HRP)-conjugated goat anti-rabbit IgG antiserum for 2 h at 4°C. After washing, the plates were incubated with O-phenylenediamine (Sigma) in PBS containing 0.01% H2O2 for 10 min at room temperature, and the reaction was stopped with 0.05 ml of 1 M HCl. The optical density at 490 nm was determined in a plate reader (Infinite M1000; Tecan).
Imai M., Watanabe T., Hatta M., Das S.C., Ozawa M., Shinya K., Zhong G., Hanson A., Katsura H., Watanabe S., Li C., Kawakami E., Yamada S., Kiso M., Suzuki Y., Maher E.A., Neumann G, & Kawaoka Y. (2012). Experimental adaptation of an influenza H5 haemagglutinin (HA) confers respiratory droplet transmission to a reassortant H5 HA/H1N1 virus in ferrets. Nature, 486(7403), 420-428.
Publication 2012
1,2-diaminobenzene anti-IgG Aves Biological Assay Centrifugation Cold Temperature Galactose Glutamic Acid Goat Homo sapiens Horseradish Peroxidase Immune Sera Influenza A Virus, H5N1 Subtype Influenza in Birds Influenzavirus A Madin Darby Canine Kidney Cells N-Acetylneuraminic Acid Parainfluenza Virus 2, Human Peroxide, Hydrogen Phosphates Poly A Rabbits Saline Solution Salts Serum Albumin, Bovine Sodium Sucrose Vertebral Column Virus Vision
2
Influenza Virus Binding Assay
Viruses were grown in MDCK cells, clarified by low-speed centrifugation, laid over a cushion of 30% sucrose in phosphate-buffered saline (PBS), and ultracentrifuged at 25,000 rpm for 2 h at 4°C. Virus stocks were aliquoted and stored at −80°C. Virus concentrations were determined by using HA assays with 0.5 % (vol/vol) TRBC. The direct receptor-binding capacity of viruses was examined by use of a solid-phase binding assay as previously described9 (link). Microtitre plates (Nunc) were incubated with the sodium salts of sialylglycopolymers [poly-L-glutamic acid backbones containing N-acetylneuraminic acid linked to galactose through either an α2,3 (Neu5Acα2,3Galβ1,4GlcNAcβ1-pAP) or an α2,6 (Neu5Acα2,6Galβ1,4GlcNAcβ1-pAP) bond] in PBS at 4°C overnight. After the glycopolymer solution was removed, the plates were blocked with 0.15 ml of PBS containing 4% bovine serum albumin (BSA) at room temperature for 1 h. Following four successive washes with ice-cold PBS, the plates were incubated in a solution containing influenza virus (8 to 32 HA units in PBS) at 4°C overnight. After washing as described above, the plates were incubated for 2 h at 4°C with rabbit polyclonal antiserum to either human H1N1 or avian H5N1 virus. The plates were then washed again as before and incubated with horseradish peroxidase (HRP)-conjugated goat anti-rabbit IgG antiserum for 2 h at 4°C. After washing, the plates were incubated with O-phenylenediamine (Sigma) in PBS containing 0.01% H2O2 for 10 min at room temperature, and the reaction was stopped with 0.05 ml of 1 M HCl. The optical density at 490 nm was determined in a plate reader (Infinite M1000; Tecan).
Imai M., Watanabe T., Hatta M., Das S.C., Ozawa M., Shinya K., Zhong G., Hanson A., Katsura H., Watanabe S., Li C., Kawakami E., Yamada S., Kiso M., Suzuki Y., Maher E.A., Neumann G, & Kawaoka Y. (2012). Experimental adaptation of an influenza H5 haemagglutinin (HA) confers respiratory droplet transmission to a reassortant H5 HA/H1N1 virus in ferrets. Nature, 486(7403), 420-428.
Publication 2012
1,2-diaminobenzene anti-IgG Aves Biological Assay Centrifugation Cold Temperature Galactose Glutamic Acid Goat Homo sapiens Horseradish Peroxidase Immune Sera Influenza A Virus, H5N1 Subtype Influenza in Birds Influenzavirus A Madin Darby Canine Kidney Cells N-Acetylneuraminic Acid Parainfluenza Virus 2, Human Peroxide, Hydrogen Phosphates Poly A Rabbits Saline Solution Salts Serum Albumin, Bovine Sodium Sucrose Vertebral Column Virus Vision
3
Multiplex Real-Time RT-PCR Assay for Respiratory Viruses

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Publication 2012
Adenovirus Infections Biological Assay Brome mosaic virus Buffers Enterovirus Enzymes Fluorescence Homo sapiens Human bocavirus Human Metapneumovirus Influenza A virus Influenza B virus NL63, Human Coronavirus Oligonucleotide Primers Para-Influenza Virus Type 1 Parainfluenza Virus 2, Human Parechovirus Plants Plant Viruses Plasmids Real-Time Polymerase Chain Reaction Respiratory Rate Respiratory Syncytial Virus Reverse Transcriptase Polymerase Chain Reaction Reverse Transcription Rhinovirus RNase P RNA Viruses Virus
4
Evaluating Influenza Virus Adaptation in Mice
Five-week-old female mice (Balb/c and DBA/J2) (Charles River Laboratories) were anaesthetized with isofluorane before intranasal inoculation with 50 µl virus suspension. In an initial evaluation, DBA/J2 and Balb/c mice (n = 4) were infected intranasally with the Ca/04 virus (5.4×105 TCID50). Body weight changes and survival were recorded daily. Mice presenting ≥25% body weight loss were humanely euthanized and counted as dead. For adaptation studies lungs were collected from DBA/J2 mice, which succumbed to infection with Ca/04 (n = 2). Lungs were homogenized in PBS with antibiotics. After centrifugation at 6,000 rpm for 10 min, 50 µl of supernatant from the homogenate was passaged to naïve Balb/c mice (n = 3). Lungs from these infected Balb/c mice were then homogenized and inoculated into MDCK cells to prepare a virus stock. The 50% mouse lethal dose (MLD50) was calculated using different virus doses in Balb/c and DBA mice (n = 3/per virus dose). Body weight and survival were recorded daily until 14 dpi. To evaluate the replication tropism of selected H1N1 pdm viruses in mice, lungs were collected at 3 and 5 dpi and titrated in MDCK cells. For histopathology analysis, mouse lungs collected at 3 dpi were fixed in 10% formalin, embedded in paraffin, sectioned and stained with hematoxylin and eosin (H&E). In order to evaluate differences in virulence of Ca/04 compared to related ma-Ca/04-derived mutants, the virus doses were adjusted to 8.0×104 TCID50/mouse.
Ye J., Sorrell E.M., Cai Y., Shao H., Xu K., Pena L., Hickman D., Song H., Angel M., Medina R.A., Manicassamy B., Garcia-Sastre A, & Perez D.R. (2010). Variations in the Hemagglutinin of the 2009 H1N1 Pandemic Virus: Potential for Strains with Altered Virulence Phenotype?. PLoS Pathogens, 6(10), e1001145.
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Publication 2010
Acclimatization Antibiotics Body Weight Centrifugation DNA Replication Eosin Females Formalin Human Body Infection Lung Madin Darby Canine Kidney Cells Mice, Inbred BALB C Mice, Inbred DBA Mus Paraffin Embedding Parainfluenza Virus 2, Human Rivers Tropism Viral Tropism Viral Vaccines Virulence Virus Virus Replication
5
Antibody Titer Determination Assays

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Publication 2009
Agglutination Antibodies, Neutralizing Biological Assay Enzymes Erythrocytes Ferrets Hemagglutination Inhibition Tests Immunoglobulins Infection Madin Darby Canine Kidney Cells Mus Parainfluenza Virus 2, Human Serum Technique, Dilution Vaccination Virus Virus Diseases

Most recents protocols related to «Parainfluenza Virus 2, Human»

1
Influenza Virus Receptor Expression in hCK Cells
The hCK cells, which are Madin–Darby canine kidney (MDCK) cells that express high levels of human-type influenza virus receptors and low levels of avian-type virus receptors [20 (link)], were cultured in minimal essential medium (MEM) containing 5% newborn calf serum (NCS) with 2 µg mL−1 puromycin and 10 µg mL−1 blasticidin at 37 °C. MDCK cells were cultured in MEM containing 5% NCS at 37 °C.
Soga T., Duong C., Pattinson D., Sakai-Tagawa Y., Tokita A., Izumida N., Nishino T., Hagiwara H., Wada N., Miyamoto Y., Kuroki H., Hayashi Y., Seki M., Kasuya N., Koga M., Adachi E., Iwatsuki-Horimoto K., Yotsuyanagi H., Yamayoshi S, & Kawaoka Y. (2023). Characterization of Influenza A(H1N1)pdm09 Viruses Isolated in the 2018–2019 and 2019–2020 Influenza Seasons in Japan. Viruses, 15(2), 535.
Full text: Click here
Publication 2023
Cells Infant, Newborn Madin Darby Canine Kidney Cells Orthomyxoviridae Parainfluenza Virus 2, Human Puromycin Serum
2
Production and Purification of HIV-Luc/VSV-G Pseudotyped Virus
To produce HIV-Luc/VSV-G pseudotyped virus, 3.5 × 106 HEK293T producer cells were transfected with 10 μg pNL4-3Luc E-R+ viral plasmid and 2 μg pMD2.G (encoding VSV-G). Virus-containing supernatant was collected 48 h post-transfection and filtered through a 0.45 μm syringe filter. The titer of the virus was measured by limiting dilution on GHOST X4/R5 reporter cells as previously described [51 (link)]. M7, M8, M9, M11, and M26 mutations were introduced into pNL4-3Luc E-R- viral plasmids, and mutant viruses were generated in a similar way. To determine the relative infectivity of progeny virions produced from EPRS knockdown cells, stable cell lines expressing EPRS-specific or control shRNAs were treated with doxycycline a day prior to transfection, and viruses were produced and titered as described above. The concentration of viral CA/p24 was measured by enzyme-linked immunosorbent assay (ELISA) using an HIV-1 p24 antigen ELISA kit (ZeptoMatrix) according to the manufacturer’s protocol. Relative infectivity was calculated as infectious unit per pg of p24.
The supernatant medium from cells (3 mL) was layered above 1 mL of 25% sucrose in TEN buffer [10 mM Tris-Cl (pH 8.0), 0.1 M NaCl, and 1 mM EDTA (pH 8.0)]. Samples were centrifuged at 100,000× g (~28,000 rpm) for 2 h at 4 °C (SW55 rotor, Beckman, Brea, CA, USA). The virus-like particle pellets were resuspended in 100 μL of 1 × SDS loading buffer, resolved by SDS-PAGE, and analyzed by Western blot.
Jin D., Zhu Y., Schubert H.L., Goff S.P, & Musier-Forsyth K. (2023). HIV-1 Gag Binds the Multi-Aminoacyl-tRNA Synthetase Complex via the EPRS Subunit. Viruses, 15(2), 474.
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Publication 2023
Antigens Buffers Cell Lines Doxycycline Edetic Acid Enzyme-Linked Immunosorbent Assay HIV-1 Infection Mutation Parainfluenza Virus 2, Human Pellets, Drug Red Cell Ghost R Factors SDS-PAGE Short Hairpin RNA Sodium Chloride Sucrose Syringes Technique, Dilution Transfection Tromethamine Virion Viroids Virus Western Blotting
3
Comprehensive Respiratory Pathogen Screening
All received swabs were tested by a BioFire® FilmArray® respiratory panel (Salt Lake City, UT, USA). The device is fully automated with the ability to perform nucleic acid purification, amplification, multiplexed PCR, and melting analysis, and generates a report for the qualitative detection of various respiratory pathogens [15 (link),16 (link)]. Screening was performed according to the manufacturer’s instructions [17 ]. An aliquot of 300 µL of the original sample swabs was uploaded into the cassette with primers for possible respiratory viral and bacterial pathogens—Adenovirus, Coronavirus 229E, Coronavirus HKU1, Coronavirus NL63, Coronavirus OC43, Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2), Human Metapneumovirus, Human Rhinovirus/Enterovirus, Influenza A, including subtypes H1, H3 and H1-2009, Influenza B, Parainfluenza Virus 1, Parainfluenza Virus 2, Parainfluenza Virus 3, Parainfluenza Virus 4, Respiratory Syncytial Virus, Bordetella parapertussis, Bordetella pertussis, Chlamydia pneumoniae and Mycoplasma pneumoniae) [17 ]. After approximately 45 min, the results were displayed by BioFire® FilmArray® Software 2.0, including that of quality control. Influenza-positive samples were subjected to an in-house-developed cycling probe real-time PCR (RT-PCR) assay using subtype/lineage-specific primers and probes.
Chon I., Saito R., Kyaw Y., Aye M.M., Setk S., Phyu W.W., Wagatsuma K., Li J., Sun Y., Otoguro T., Win S.M., Yoshioka S., Win N.C., Ja L.D., Tin H.H, & Watanabe H. (2023). Whole-Genome Analysis of Influenza A(H3N2) and B/Victoria Viruses Detected in Myanmar during the COVID-19 Pandemic in 2021. Viruses, 15(2), 583.
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Publication 2023
Adenovirus Infections Bacteria Biological Assay Bordetella parapertussis Bordetella pertussis Chlamydophila pneumoniae Coronavirus Coronavirus 229E, Human Enterovirus Homo sapiens Human Metapneumovirus Influenza Medical Devices Multiplex Polymerase Chain Reaction Mycoplasma pneumoniae NL63, Human Coronavirus Nucleic Acids Oligonucleotide Primers Para-Influenza Virus Type 1 Para-Influenza Virus Type 3 Parainfluenza Virus 2, Human Parainfluenza Virus 4, Human Pathogenicity Real-Time Polymerase Chain Reaction Respiratory Rate Respiratory Syncytial Virus Rhinovirus SARS-CoV-2 Sodium Chloride
4
Caffeic Acid Disrupts ILHV Replication
Time-of-drug addition were performed to explore which steps of the ILHV replication cycle are blocked by caffeic acid. Briefly, CA was added to the virus and/or host cells at different times before, during, and after viral inoculation into the cells as follows (Figure 1): (1) pre-treatment of virus followed by inoculation of the treated virus into the cells investigates whether CA has virucidal or neutralizing activity; (2) pre-treatment of the cells with CA before viral inoculation explores whether this substance could block the viral receptor, inhibiting viral attachment to the host cells, or if it could induce production of antiviral host factors; (3) co-treatment of cells and virus during virus inoculation examines the function of CA during the steps of virus entry, including virucidal (neutralizing) activity and blockade of viral attachment and penetration into the cells; (4) treatment of virus-infected cells during the entire post-inoculation period investigates the antiviral effects of CA during post-entry steps such as genome translation and replication, virion assembly, and virion release from the cells. Viral infection experiments were performed in A549, HepG2, or Vero cells seeded in 24-well plates treated with CA or untreated controls. Under the different conditions described above, the cells were infected with MOI 1 of ILHV for one hour at 37 °C and revealed through the virus plaque-forming assay titration of supernatant or cell content (described in Section 2.4). Three independent experiments with quadruplicate measurements were performed. Data were analyzed by four-parameter curve fitting from a dose–response curve using GraphPad Prism (version 8.00) to calculate EC50 (concentration of the compound that inhibited 50% of the infection), and the selectivity index for the compound was calculated as the CC50:EC50 ratio.
Saivish M.V., Pacca C.C., da Costa V.G., de Lima Menezes G., da Silva R.A., Nebo L., da Silva G.C., de Aguiar Milhim B.H., da Silva Teixeira I., Henrique T., Mistrão N.F., Hernandes V.M., Zini N., de Carvalho A.C., Fontoura M.A., Rahal P., Sacchetto L., Marques R.E, & Nogueira M.L. (2023). Caffeic Acid Has Antiviral Activity against Ilhéus Virus In Vitro. Viruses, 15(2), 494.
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Publication 2023
Antiviral Agents caffeic acid Cells DNA Replication Genetic Selection Genome Infection Parainfluenza Virus 2, Human Pharmaceutical Preparations prisma Receptors, Virus Somatostatin-Secreting Cells Titrimetry Vaccination Vero Cells Viral Plaque Assay Viral Vaccines Virion Virus Virus Assembly Virus Attachment Virus Diseases Virus Internalization
5
Immunoprecipitation Assay for Influenza A Virus
To determine the application of mAb 5F10 in IP assay, an avian H5N6 virus from group 1 subtypes and an avian H3N2 virus from group 2 subtypes of IAV (Sangesland and Lingwood 2021 (link)) were selected as representatives for the experiment. MDCK cells were infected with IAV H3N2 or H5N6 at 1 MOI. At 24 h post-infection, the cells were lysed in IP buffer (#P0013, Beyotime, China) and then incubated with 3 µg mAb 5F10 or IgG1 isotype (#5415, Cell Signaling Technology, USA) for 30 min at 37 °C. After addition of the protein A+G magnetic beads (#P2108, Beyotime, China), the lysates were incubated at 4 °C overnight. Subsequently, the protein complex bound to the beads was then eluted into 5× sodium dodecyl sulfate (SDS) loading buffer (#P0015, Beyotime, China). Finally, the immunoprecipitated proteins were analyzed by western blot with mAb 5F10 as the primary antibody and HRP-labeled goat anti-mouse IgG (#CW0102, CWBIO, China) as the secondary antibody.
Gu M., Jiao J., Liu S., Zhao W., Ge Z., Cai K., Xu L., He D., Zhang X., Qi X., Jiang W., Zhang P., Wang X., Hu S, & Liu X. (2023). Monoclonal antibody targeting a novel linear epitope on nucleoprotein confers pan-reactivity to influenza A virus. Applied Microbiology and Biotechnology, 107(7-8), 2437-2450.
Publication 2023
anti-IgG Biological Assay Buffers Cells G-substrate Goat GTP-Binding Proteins IgG1 Immunoglobulin Isotypes Immunoglobulins Infection Madin Darby Canine Kidney Cells Mus Parainfluenza Virus 2, Human Proteins Staphylococcal Protein A Sulfate, Sodium Dodecyl Western Blotting

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More about "Parainfluenza Virus 2, Human"

Parainfluenza Virus 2, also known as PIV2, is a member of the Paramyxoviridae family and is a common cause of respiratory infections in humans.
This virus primarily affects young children and can lead to severe illnesses, especially in immunocompromised individuals.
Parainfluenza Virus 2 is transmitted through respiratory droplets and can cause croup, bronchiolitis, and pneumonia.
Conducting research on Parainfluenza Virus 2 is crucial for developing effective treatment and prevention strategies.
Researchers can utilize various techniques and reagents to study this virus, such as TRIzol reagent for RNA extraction, SYBR Premix Ex Taq II for real-time PCR, and DMEM with L-glutamine for cell culture.
Additionally, the use of AMV reverse transcriptase and FBS can be helpful in the study of Parainfluenza Virus 2.
To enhance research efficiency and accuracy, researchers can leverage tools like the Anyplex™ Respiratory Panel Assays and the Opti-MEM media.
These resources can assist in the detection and identification of Parainfluenza Virus 2, as well as other respiratory viruses.
Furthermore, the PubCompare.ai platform can help researchers optimize their studies by comparing protocols from literature, preprints, and patents, enabling them to identify the most reproducible and accurate methods.
By understanding the latest research on Parainfluenza Virus 2 and utilizing the appropriate techniques and tools, researchers can contribute to the development of effective treatments and prevention strategies, ultimately improving the health and well-being of those affected by this respiratory virus.