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AB94965

Anti-Respiratory Syncytial Virus Phosphoprotein antibody [RSVH102]

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(12 Publications)

Mouse Monoclonal PHOSP antibody. Suitable for IP, ELISA, WB, ICC/IF, IHC-Fr and reacts with Respiratory syncytial virus samples. Cited in 12 publications. Immunogen corresponding to Cell preparation containing Respiratory Syncytial Virus Phosphoprotein protein.

View Alternative Names

Phosphoprotein, Protein P, P

Key facts

Host species

Mouse

Clonality

Monoclonal

Clone number

RSVH102

Isotype

IgG1

Carrier free

No

Reacts with

Respiratory syncytial virus

Applications

ELISA, IHC-Fr, IP, WB, ICC/IF

applications

Immunogen

The exact immunogen used to generate this antibody is proprietary information.

Specificity

ab94965 has broad specificity for Human Respiratory Syncytial Virus of both sub-groups A and B.

Reactivity data

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Product details

Fusion partner: PS-NS/1-Ag4

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein A
Storage buffer
Preservative: 0.02% Sodium azide Constituents: PBS
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The Respiratory Syncytial Virus (RSV) Phosphoprotein also known as P or M2-1 protein acts mechanically as an important component of the virus's RNA synthesis machinery. It is a nonstructural protein with a molecular mass of approximately 27 kDa. The phosphoprotein is expressed abundantly in infected host cells during RSV replication. Functionally its primary role involves forming a complex with the RSV nucleoprotein and the large polymerase protein which are essential for viral RNA transcription and replication.
Biological function summary

The RSV Phosphoprotein plays a significant role in stabilizing the RNA polymerase complex during viral gene expression. This protein does not act alone; it is part of a larger ribonucleoprotein complex that ensures efficient transcription of viral mRNA. It facilitates the assembly of enzyme components on the viral genome promoting fidelity in the transcription and replication processes which is important for the virus's infectivity.

Pathways

The RSV Phosphoprotein is deeply involved in the viral assembly and replication pathway. It interacts primarily with the nucleoprotein (N) and the polymerase protein (L) forming an active transcription complex. This protein coordinates processes within the viral life cycle such as replication and viral assembly directly impacting protein interactions that guide the synthesis of new viral particles within the RSV replication pathway.

RSV Phosphoprotein is linked to respiratory tract infections like bronchiolitis and pneumonia. Its interaction with nucleoprotein and polymerase protein not only contributes to the virus's ability to propagate but also helps evade host immune responses making it a target for antiviral interventions. Understanding this protein's interactions with other RSV-specific proteins opens possibilities for therapeutic development targeting respiratory diseases.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Plays critical roles in regulating RNA replication and transcription through its interactions with multiple proteins (PubMed : 25568210, PubMed : 26474524). Tethers the RNA-directed RNA polymerase L to the nucleoprotein-RNA complex (PubMed : 26474524). Recruits the M2-1 protein, a processivity factor that is required for efficient transcription of viral RNA (PubMed : 26474524). Acts as a chaperone for neo-synthesized nucleoprotein by forming an N-P complex that preserves N in a monomeric and RNA-free state and prevents the association of nascent N with host cell RNAs (PubMed : 25568210). Recruits the host phosphatase PP1 to inclusion bodies to regulate viral transcription (PubMed : 29489893). Together with the nucleoprotein, sequesters host NF-kappa-B in inclusion bodies (IBs) thereby inhibiting this host defense pathway (By similarity).
See full target information P

Publications (12)

Recent publications for all applications. Explore the full list and refine your search

Virology journal 22:244 PubMed40665364

2025

Respiratory syncytial virus (RSV) enhances translation of virus-resembling AU-rich host transcripts.

Applications

Unspecified application

Species

Unspecified reactive species

Kyra Kerkhofs,Nicholas R Guydosh,Mark A Bayfield

PLoS pathogens 20:e1012198 PubMed38739647

2024

Intranasal respiratory syncytial virus vaccine attenuated by codon-pair deoptimization of seven open reading frames is genetically stable and elicits mucosal and systemic immunity and protection against challenge virus replication in hamsters.

Applications

Unspecified application

Species

Unspecified reactive species

Megan Levy,Jessica W Chen,Jaclyn A Kaiser,Hong-Su Park,Xueqiao Liu,Lijuan Yang,Celia Santos,Ursula J Buchholz,Cyril Le Nouën

mBio 14:e0148023 PubMed37909764

2023

The nonstructural protein 1 of respiratory syncytial virus hijacks host mitophagy as a novel mitophagy receptor to evade the type I IFN response in HEp-2 cells.

Applications

Unspecified application

Species

Unspecified reactive species

Jing Cheng,Yutong Wang,Lizheng Yin,Wenzhang Liang,Jing Zhang,Cuiqing Ma,Yu Zhang,Bo Liu,Jiachao Wang,Weiting Zhao,Miao Li,Lin Wei

PloS one 18:e0289100 PubMed37490507

2023

The respiratory syncytial virus M2-2 protein is targeted for proteasome degradation and inhibits translation and stress granules assembly.

Applications

Unspecified application

Species

Unspecified reactive species

Orlando Bonito Scudero,Verônica Feijoli Santiago,Giuseppe Palmisano,Fernando Moreira Simabuco,Armando Morais Ventura

Microbiology and immunology 67:413-421 PubMed37424190

2023

Establishment of a new reverse genetics system for respiratory syncytial virus under the control of RNA polymerase II.

Applications

Unspecified application

Species

Unspecified reactive species

Tatsuki Takahashi,Shiori Ueno,Yoshiro Sugiura,Kenta Shimizu,Wataru Kamitani

Virus research 327:199060 PubMed36746339

2023

RSV-induced expanded ciliated cells contribute to bronchial wall thickening.

Applications

Unspecified application

Species

Unspecified reactive species

Sattya N Talukdar,Jaspreet Osan,Ken Ryan,Bryon Grove,Danielle Perley,Bony D Kumar,Shirley Yang,Sydney Dallman,Lauren Hollingsworth,Kristina L Bailey,Masfique Mehedi

PLoS pathogens 16:e1008987 PubMed33031461

2020

Polymerase-tagged respiratory syncytial virus reveals a dynamic rearrangement of the ribonucleocapsid complex during infection.

Applications

Unspecified application

Species

Unspecified reactive species

Emmeline L Blanchard,Molly R Braun,Aaron W Lifland,Barbara Ludeke,Sarah L Noton,Daryll Vanover,Chiara Zurla,Rachel Fearns,Philip J Santangelo

Cellular microbiology 21:e12955 PubMed30223301

2018

Late activation of the Raf/MEK/ERK pathway is required for translocation of the respiratory syncytial virus F protein to the plasma membrane and efficient viral replication.

Applications

Unspecified application

Species

Unspecified reactive species

Hannah F Preugschas,Eike R Hrincius,Carolin Mewis,Giao V Q Tran,Stephan Ludwig,Christina Ehrhardt

Journal of virology 92: PubMed29386287

2018

Respiratory Syncytial Virus Replication Is Promoted by Autophagy-Mediated Inhibition of Apoptosis.

Applications

Unspecified application

Species

Unspecified reactive species

Miao Li,Jian Li,Ruihong Zeng,Jianling Yang,Jianguo Liu,Zhengzheng Zhang,Xiaotian Song,Zhiyan Yao,Cuiqing Ma,Wenjian Li,Kai Wang,Lin Wei

Journal of virological methods 254:51-64 PubMed29410056

2018

Evaluation of monoclonal antibodies that detect conserved proteins from Respiratory Syncytial Virus, Metapneumovirus and Adenovirus in human samples.

Applications

ICC/IF, ELISA

Species

Unspecified reactive species, Unspecified reactive species

Liliana A González,Yaneisi Vázquez,Jorge E Mora,Christian E Palavecino,Pablo Bertrand,Marcela Ferrés,Ana M Contreras,Andrea A Beckhaus,Claudia A Riedel,Susan M Bueno
View all publications

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