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Written by | November
The adaptive immune system of vertebrates modifies the genome of individual B cells, encoding antibodies that bind to specific antigens [1], and is the Monkey King in the human body, with seventy-two changes
.
In most mammals, antibodies consist of heavy and light chains, produced sequentially by the recombination of V, D, J, and C gene segments
.
Each strand contains three complementary determining regions (CDR1–CDR3), which help antigens develop specificity
.
Specific combinations of heavy and light chains are preferred for certain antigens, but is there a pattern to this combination?
On October 26, 2022, the research group of Wyatt J.
McDonnell of 10x Genomics in the United States collaborated with David B.
Jaffe (first author) to publish the article Functional antibodies exhibit in Nature Light chain coherence, found that for initial antibodies, the probability of using the common light chain V gene is 0%, but for memory function antibodies, the probability rises to 80%.
The authors call this discovery Light chain coherence, a phenomenon determined by heavy
chains.
One of the core challenges in immunology is classifying
antibodies by function.
In practice, it is possible to test a small number of antibodies in vitro and a simple binding
to a specific antigen using a large number of antibody tests.
If the characteristics of antibodies can be understood on a large scale only from the sequence information of antibodies in the future, it will be of great help
to the grouping and function of antibodies by map.
However, large databases of multiple antigen-specific antibodies are lacking, making it difficult to assess
the effectiveness of any existing functional grouping.
Nature is always full of wisdom that replicates antibodies by clone types with the same function and combines
these replicas.
The reproduction of sequence similarity in antibodies has aroused the research interest
of the authors.
The authors first divided antibody sequences into two types by calculation: naive antibody and memory antibody
.
First, by inferring the V gene allele, it is estimated that the B cell allele occurs outside the junction region Somatic hypermutations (SHMs), if an antibody sequence does not have somatic high mutations, it is considered an initial antibody, and if present, it is considered a memory function antibody
.
The authors then wanted to explore whether similar heavy chains in unrelated B cells meant similar light chains
.
The authors analyzed antibodies in naïve B cells and memory B cells, taking into account pairs
of cells with the same heavy chain V gene, the same length of CDRH3, and cells from different donors.
The consistency of light chains in each group of cells is then calculated, i.
e.
, the percentage of cell pairs with the same name of the
light chain genes.
The authors found that in the initial B cells, the proportion of light chain consistency was 10 percent, and in memory B cells, the proportion rose to 82 percent
.
Further, the authors analyzed multiple published databases and found a widespread 79%-93% consistency
in memory B cells.
This suggests that there is a high degree of light chain consistency
for memory B cells.
Classifying antibodies based on a given CDRH3 amino acid sequence type, the authors found that the same heavy chains were needed to classify them at the same time, so that antibodies could be effectively classified
by sequence.
Therefore, the heavy chain in antibody function determines the light chain
to a certain extent.
In nature, many heavy chain configurations effectively bind to a given antibody target
.
For each heavy chain configuration, the determination rate of homologous light chains at the level of light chain genes or similar genes is about 80%, and the authors confirm this view
by the probability of heavy chain reproduction.
In general, the authors' work found that there is no specific pattern of light chains when initial B cells produce antibodies that do not yet function, but memory B cells show broad light chain consistency after producing functional antibodies, which is the characteristic of
antibody acquisition function and selection.
This discovery provides a new perspective
for the functional classification of antibodies.
Original link:
https://doi.
org/10.
1038/s41586-022-05371-z
Pattern maker: Eleven
References
1.
Tonegawa, S.
Somatic generation of antibody diversity.
Nature 302, 575–581 (1983).
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