Q.29 Which one of the following is NOT TRUE for class I MHC protein?
(A) MHC class I protein are polymorphic
(B) T-cell receptors recognizes MHC class I protein
(C) MHC class I protein are displayed on the surfaces of nucleated vertebrate cells
(D) 𝛽2 -microglobulin is covalently associated with MHC class I protein
Option (D) is NOT TRUE for class I MHC protein.
MHC class I proteins present intracellular peptides to cytotoxic T cells on nucleated cells. This question tests key structural and functional features relevant for CSIR NET Life Sciences.
Option Analysis
(A) MHC class I proteins are polymorphic
MHC class I genes, such as HLA-A, -B, and -C in humans, exhibit high polymorphism with numerous alleles in populations. This diversity enables presentation of varied peptides, enhancing immune response variability. Thus, this statement is true.
(B) T-cell receptors recognize MHC class I protein
T-cell receptors (TCRs) on CD8+ cytotoxic T cells bind peptide-loaded MHC class I complexes. Recognition triggers immune responses against infected or abnormal cells. This statement holds true.
(C) MHC class I proteins are displayed on nucleated vertebrate cells
These proteins appear on nearly all nucleated cells, including platelets in some cases, to signal intracellular status. Non-nucleated cells like mature erythrocytes lack them. This is accurate.
(D) β2-microglobulin is covalently associated with MHC class I protein
β2-microglobulin (β2m) forms a heterodimer with the MHC class I heavy chain via non-covalent interactions. No covalent bond exists; engineered exceptions confirm natural non-covalent association. This statement is false.
Class I MHC proteins play a vital role in immune surveillance by presenting peptides to T cells. For CSIR NET aspirants, understanding what is NOT true for class I MHC protein clarifies key misconceptions in immunology. This guide breaks down the MCQ options on class I MHC protein characteristics.
Core Features of Class I MHC Protein
Class I MHC proteins consist of a polymorphic heavy chain and non-covalently bound β2-microglobulin. They display endogenous peptides on nucleated vertebrate cells for TCR scrutiny.
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High polymorphism in α chain genes ensures diverse peptide binding.
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TCRs recognize peptide-MHC complexes, activating CD8+ T cells.
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Expressed ubiquitously on nucleated cells, absent on erythrocytes.
Why β2-Microglobulin is NOT Covalently Associated
The false statement claims covalent linkage, but β2m associates non-covalently with the heavy chain’s α3 domain. Crystal structures confirm this interaction supports stability without bonds. Dissociation occurs under stress, unlike covalent pairs.
Exam Relevance for CSIR NET
This MCQ tests MHC structure and function, common in Unit 10 (Immunology). Polymorphism aids pathogen evasion challenges; non-covalent β2m enables dynamic assembly. Master these for competitive edges in genetics and biotech sections.


