맨위로가기

RIG-I

"오늘의AI위키"는 AI 기술로 일관성 있고 체계적인 최신 지식을 제공하는 혁신 플랫폼입니다.
"오늘의AI위키"의 AI를 통해 더욱 풍부하고 폭넓은 지식 경험을 누리세요.

1. 본문

RIG-I (Retinoic acid-inducible gene I) is a crucial component of the innate immune system, acting as a cytosolic pattern recognition receptor (PRR). It plays a key role in detecting viral infections and triggering an antiviral response. Here's a breakdown of RIG-I:
Function:


  • Viral RNA Sensor: RIG-I primarily senses viral RNA in the cytoplasm of cells. It specifically recognizes:
  • Short double-stranded RNA (dsRNA).
  • Single-stranded RNA (ssRNA) with a 5'-triphosphate end, a characteristic often found in viral RNA but not in host RNA.
  • Initiates Antiviral Response: Upon binding to viral RNA, RIG-I undergoes conformational changes and activates a signaling cascade.
  • Type I Interferon Production: This cascade leads to the production of type I interferons (IFNs), primarily IFN-α and IFN-β. Type I IFNs are critical for:
  • Limiting viral spread to neighboring cells.
  • Promoting an innate immune response, including inflammation.
  • Activating the adaptive immune system.
  • Pro-inflammatory Cytokine Production: Besides IFNs, RIG-I activation also stimulates the production of pro-inflammatory cytokines, further enhancing the immune response.
  • Detects various viruses including, West Nile virus, Japanese Encephalitis virus, influenza A, Sendai virus, flavivirus, and coronaviruses

Structure:

  • Encoded by: The *DDX58* gene in humans.
  • Domains:
  • CARDs (Caspase Activation and Recruitment Domains): Two N-terminal CARDs are essential for interacting with the adaptor protein MAVS (mitochondrial antiviral signaling protein), also known as VISA, Cardif, or IPS-1.
  • Helicase Domain: A central ATP-dependent DExD/H box RNA helicase domain is responsible for binding to RNA and unwinding it.
  • CTD (C-terminal Domain) and RD (Repressor Domain): The C-terminal domain (CTD) binds to viral RNA, while the repressor domain (RD) regulates RIG-I activity.

Mechanism of Activation:1. Recognition: In the resting state, RIG-I is auto-inhibited. Upon viral infection, the CTD of RIG-I binds to viral RNA (short dsRNA or 5'-triphosphate ssRNA).

2. Conformational Change: RNA binding leads to a conformational change, exposing the CARD domains.

3. Oligomerization: RIG-I forms a complex with the viral RNA and then undergoes homooligomerization, forming filaments.

4. MAVS Interaction: The exposed CARD domains of RIG-I interact with the CARD domains of MAVS, which is located on the mitochondria.

5. Signal Transduction: MAVS acts as an adaptor protein, recruiting downstream signaling molecules like TBK1 (TANK-binding kinase 1) and IKK (IκB kinase).

6. Transcription Factor Activation: These kinases phosphorylate and activate transcription factors, including IRF3 (interferon regulatory factor 3), IRF7, and NF-κB (nuclear factor kappa-light-chain-enhancer of activated B cells).

7. Interferon and Cytokine Production: The activated transcription factors move to the nucleus and induce the expression of type I interferons (IFN-α and IFN-β) and other pro-inflammatory cytokines.
Regulation:

  • RIG-I expression can be induced by various factors, including retinoic acid, lipopolysaccharide (LPS), IFN, and viral infection itself.
  • It has been found that RIG-I activation can also cause damage to organs and tissues.
  • Self-RNAs do not activate RIG-I signaling because their 5'ppp is capped by 2'O-methylation.

Other Roles:Besides its antiviral functions, there's evidence that RIG-I may also be involved in:

  • Granulocyte production and differentiation.
  • Bacterial phagocytosis.
  • Regulation of cell migration.
  • Responding to cytosolic DNA.
  • Inflammation related to non-viral triggers like LPS and certain cytokines.
  • Plays a role in macrophage activation.


RIG-I is part of a family of receptors called RIG-I-like receptors (RLRs), which also includes MDA5 (Melanoma Differentiation-Associated protein 5) and LGP2 (Laboratory of genetics physiology 2).



본 사이트는 AI가 위키백과와 뉴스 기사,정부 간행물,학술 논문등을 바탕으로 정보를 가공하여 제공하는 백과사전형 서비스입니다.
모든 문서는 AI에 의해 자동 생성되며, CC BY-SA 4.0 라이선스에 따라 이용할 수 있습니다.
하지만, 위키백과나 뉴스 기사 자체에 오류, 부정확한 정보, 또는 가짜 뉴스가 포함될 수 있으며, AI는 이러한 내용을 완벽하게 걸러내지 못할 수 있습니다.
따라서 제공되는 정보에 일부 오류나 편향이 있을 수 있으므로, 중요한 정보는 반드시 다른 출처를 통해 교차 검증하시기 바랍니다.

문의하기 : help@durumis.com