lecture 10 true and false quiz- immunology

Peptide antigens for Class I MHC molecules are generated from extracellular proteins.

The proteasome is responsible for breaking down proteins into smaller peptides during antigen processing.

The TAP complex is involved in loading peptides onto Class I MHC molecules.

The MHC cell surface proteins present lipids to T cell receptors.

T cell receptors only recognize the peptide portion and not the MHC portion.

T cell receptors (TCRs) only recognize peptide antigens, not protein antigens.

MHC molecules are also known as Major Histocompatibility Complex (MHC) in humans.

Class I MHC molecules present peptides derived from extracellular proteins to CD4+ helper T cells.

Each T cell receptor (TCR) is specific to a particular MHC-peptide complex.

The interaction between the TCR and the MHC-peptide complex is non-specific.

Peptide antigens presented by Class I MHC molecules can originate from both extracellular and cytosolic proteins.

The proteasome degrades proteins into longer peptide fragments, typically 15-20 amino acids in length.

The TAP complex is responsible for transporting peptide fragments from the ER into the cytosol.

Class I MHC molecules consist of a heavy chain, an alpha chain, and a beta chain.

The MHC-peptide interaction plays a crucial role in activating B cells.

Peptide antigens presented by Class I MHC molecules come from extracellular proteins.

The antigen processing pathway for Class II MHC molecules involves loading of peptides onto newly synthesized MHC molecules.

The TAP complex functions in delivering peptides from the ER to the cytosol.

MHC cell surface proteins present lipids to T cell receptors.

T cell receptors only recognize peptide antigens but not the MHC molecules.

Peptide-binding cleft of Class I MHC molecules is initially empty during biosynthesis.

Peptide antigens are transported by TAP into the ER to be loaded onto Class I MHC molecules.

Peptides with low affinity to Class I MHC molecules are selectively retained.

Peptide-MHC complexes are transported from the Golgi apparatus to the ER.

CD8+ CTLs recognize the peptide-MHC complexes displayed on the cell surface.

The TCR recognizes both the peptide antigen and the MHC molecule.

Proteasome is responsible for breaking down proteins into smaller peptides during antigen processing.

Protein antigens are presented to T cells by MHC cell surface proteins.

The TAP complex is involved in loading peptides onto Class I MHC molecules.

MHC molecular structure is a stable timer that triggers T cell responses.

Class I MHC molecules only present peptides derived from intracellular proteins to CD4+ helper T cells.

The proteasome is responsible for breaking down proteins into smaller peptides during antigen processing.

MHC cell surface proteins present lipids to T cell receptors.

The interaction between the TCR and the MHC-peptide complex is non-specific.

There are three main classes of MHC cell surface proteins.

Every protein antigen contains many potential epitopes.

T cell receptors only recognize the peptide portion and not the MHC portion.

MHC molecular structure, once fully assembled, remains stable and does not change.

Class II MHC molecules are primarily involved in presenting peptides derived from intracellular proteins.

The TAP complex is involved in loading peptides onto Class II MHC molecules.