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Flashcards

5 - antigen processing and presentation

Georgie Philpott Biomedicine Year 2 Year 2 English 45 cards

Cards in this deck (45)

  1. 1what is pathogenic neutralisationpathogens evolve to no longer compliment the antibody
  2. 2which antibody can cross epithelial surface and enter nucleusIgA
  3. 3give two examples of pathogens that can enter cells and therefore hide from the immune systemviruses and microbacteria like TB
  4. 4what kind of infection do CD4+ T cells handleintravesicular and extracellular antigens
  5. 5what kind of infection do CD8+ T cells handle/protect againstcytosolic pathogens (viruses and cancer)
  6. 6which T cell processes and presents vescicular pathogensCD4 T helper cell (1)
  7. 7specifically what do CD8+ T cells dokill the virally infected cell before the virus can replicate
  8. 8when a CD4+ T cell detect intravesicular pathogens what do they doproduce interferon gamma which activates macrophages to kill pathogens inside the vesicle
  9. 9when CD4+ T cell detects extracellular pathogens what does it doactivates B cells to make antibodies (Ig)
  10. 10what do B cells need to undergo and how does it happen?affinity maturation
    T cell binds to it and also produces cytokines signalling which pathogen it is
  11. 11how do B cells also activate CD4 T cellsby acting as an APC and presenting antigen on MHC II to T cells so that the T cell can provide cytokines for B cell maturation
  12. 12what does MHC stand formajor histocompatibility complex
  13. 13what do both MHC classes bindpeptide fragments of an antigen
  14. 14describe the type of peptide fragment MHC class 1 presents and why?shorter peptides as the end of the MHC cleft are restrictive
  15. 15describe the type of peptide fragment MHC class 2 presents and why?bigger peptides as ends of cleft are open
    but this gets degraded down by exopeptidases
  16. 16why are some people better protected against pathogens than others?MHC molecules are highly polymorphic
    different MHC bind different molecules
  17. 17describe the structure of MHC class 1 molecule3 domains - alpha 1, 2, 3
    1+2 are binding cleft
    one transmembrane domain (3)
  18. 18where on MHC class 1 are the polymorphisms foundalpha 1 + 2 domains
  19. 19describe the structure of MHC class 2 molecule2 chains - alpha and beta
  20. 20what is HLADR and where are all its polymorphisms?human MHC 2 molecule +
    polymorphisms on its beta chain
  21. 21generally speaking where are the polymorphisms found on all MHC moleculespeptide-binding groove (outer domains)
  22. 22what do these polymorphisms determinewhich antigen peptide will bind to that specific MHC molecule
  23. 23what is bound to the MHC class 2 whilst it is being processedinvarient chain
  24. 24what is the purpose of the invarient chain?to protect the binding sight of the MHC class 2 and stop anything else binding until it is fully formed
  25. 25what molecule binds to the the subunits of MHC class 2 + aid in formation and folding (including the invarient chain formation)? where does this take place?chaperone proteins
    bind to asparagine-linked sugar side chains on side of molecules
    ER
  26. 26when is the MHC class 2 released from the golgi?when it is folded and formed properly
  27. 27example of chaperone proteincalnexin
  28. 28which part of invarient chain sits in the MHC cleft80-100 amino acids
  29. 29what is the structure that then enters the endosometrimerization domain
    3 MHC class 2
    3 invarient chains
  30. 30what then cleaves the invarient chain bound to the MHC class 2 molecule and exogenous proteins in the endosome from the endocytic pathwayproteolytic enzymes e.g. cathepsin
  31. 31what is the cleaved section of invarient chain that is left in the MHC class 2 binding domain called?CLIP molecule
  32. 32what catalyses the swap of antigenic peptide for CLIPchaperone HLA-DM
  33. 33what the final stage of the MIIC pathwaymovement of the loaded MHC class II molecule to the plasma membrane to present antigen peptide to CD4+ T cells
  34. 34what transporters sit on the ER and pump peptides into the ERTAP
  35. 35how are defective ribosomal products removed from teh cellubiquitylation
    in proteosome to break the protein into short fragments
  36. 36what is the name of the proteosome that is involved in antigen presentation on MHC class 1immunoproteosome
  37. 37where does this proteosome cleave the peptides and what is this because ofafter hydrophobic and basic residues due to the LMP molecules in its structure
  38. 38immunoproteosomes produce peptides, virus particles and intracellular pathogens, where do these go next?to the TAP proteins on the ER and get pumped into the ER
  39. 39how is MHC class 1 inserted into the ERsignal recognition pore
  40. 40what is bound to the MHC class 1 molecule in the ERchaperone proteins --> calnexin
  41. 41what does calnexin get replaced forcalreticulum
  42. 42what process occurs to ensure that the peptides bind strongly to the MHC class 1 moleculeoxidoreductase hits disulphide bonds and destabilises molecule which strengthens bond
  43. 43when is the MHC class 1 released and presented on cell membrane?when a peptide has bound with high enough affinity
  44. 44what is cross presentation? what controls thiswhen exogenous antigens are presented on MHC class 1
    TLR signals control this
  45. 45what is exogenous antigen presentation through cross presentation not efficient forcytotoxic T cell killing of infected cell

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Year 2 Biomedicine Year 2 (Immunity and infection ) Flashcards on 5 - antigen processing and presentation, created by Georgie Philpott on 18/12/2022.
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