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Related Concept Videos

Antigen Processing Pathways01:31

Antigen Processing Pathways

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MHC molecules are key players in the immune response, enabling T cells to recognize and respond to specific antigens. They are present on the surface of all nucleated cells in the body and are instrumental in presenting antigens to T cells and activating them. T cells recognize the MHC-antigen complex and initiate an immune response. MHC class I and MHC class II are two main types of MHC molecules, each associated with a distinct antigen processing pathway.
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An antigen is any substance the immune system identifies as foreign and potentially harmful to the body, prompting an immune response. Antigens have two functional properties: immunogenicity and reactivity. Immunogenicity is the ability of an antigen to stimulate a specific immune response. At the same time, reactivity describes the antigen's ability to react with the cells and antibodies produced in response to it.
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Protein Complex Assembly02:41

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Translocation of Proteins into the Mitochondria01:19

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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
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Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...
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Protein Translocation Machinery on the ER Membrane

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The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
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Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin
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Structure of the human MHC-I peptide-loading complex.

Andreas Blees1, Dovile Januliene2, Tommy Hofmann3

  • 1Institute of Biochemistry, Biocenter, Goethe University Frankfurt, Max-von-Laue Strasse 9, 60438 Frankfurt/Main, Germany.

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The peptide-loading complex (PLC) structure reveals how it coordinates peptide transport and MHC-I loading for immune responses. This reveals the molecular basis of adaptive immunity initiation.

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Area of Science:

  • Immunology
  • Structural Biology
  • Molecular Cell Biology

Background:

  • The peptide-loading complex (PLC) is crucial for adaptive immunity, assembling peptide-MHC-I complexes in the endoplasmic reticulum.
  • Its dynamic and heterogeneous nature has previously hindered structural and mechanistic studies.

Purpose of the Study:

  • To determine the native structure and molecular organization of the human peptide-loading complex (PLC).
  • To elucidate the mechanism of major histocompatibility complex class I (MHC-I) assembly and peptide loading.

Main Methods:

  • Isolation of human PLC from Burkitt's lymphoma cells using a viral inhibitor.
  • Determination of native PLC structure via cryo-electron microscopy (cryo-EM).
  • Analysis of distinct assembly states to understand dynamic processes.

Main Results:

  • Revealed a pseudo-symmetric arrangement of two editing modules (tapasin, calreticulin, ERp57, MHC-I) around the transporter associated with antigen processing (TAP).
  • Identified a chaperone network facilitating MHC-I proofreading and peptide editing.
  • Described the translocation pathway of TAP and peptide channeling to MHC-I.

Conclusions:

  • The study defines the molecular architecture of the PLC, revealing the interplay between TAP and chaperone networks in MHC-I assembly.
  • Provides mechanistic insights into MHC-I recruitment, editing, and release, crucial for initiating adaptive immune responses.