Introduction
Scientific advancements have enabled antibodies that identify non-changing structures of the protein of influenza haemagglutinin (HA) to be identifiable. This development has strengthened the efforts of developing universal influenza vaccines. The goal of this research is to find out how HA stimulates naïve B cells into maturation and induces protective immunity. The researchers chose to investigate this phenomenon because the antibodies that can be used for the vaccine derive from a particular antibody gene of the region IGHV1-69. Currently, the manner in which influenza haemagglutinin stimulates naïve B cells into maturation and protective immunity remains unknown. This essay integrates molecular biology knowledge in examining the article by Lingwood, Mctamney, Yassine, Whittle, Guo, Boyington, Wei, and Nabel., in terms of objectives, findings, and conclusion.
The research by Lingwood et al. comprised of various tests and investigations. First, the researchers wanted to define the molecular explanation behind the antibodies’ affinity maturation. They analyzed the contributions made by light and heavy chains in antigen recognition. They completed this process by comparing chimaeric antibodies comprising of germline light (gL) and somatic heavy (sH) chains to a mature antibody (sHsL). The finding was that the chimaeric sHgL of the three antibodies bound to the recombinant H1HA, bearing affinities that were similar to their mature sHgL. They discovered that maturation of the gL chain did not affect the binding to H1 HA. The somatic mutation of the heavy chain gene IGHV1-69 alone mediates the increment in binding affinity. The researchers identified this finding as consistent with the observations made in the crystal structures of the complexes known as CR6261–HA and F10–HA.
The next investigation was the minimum requirements needed for heavy chain loop maturation that contributes to somatic activity. The researchers focused their analysis on CR6261, an anti-stem of IGHV1-69 antibody. Their findings in this investigation suggest that potential neutralization may emerge as a result of the mutation of a small portion of the germline residues.
One major finding of the study is that IGHV1-69 antibodies engage HA with adequate affinity to cause B-cell activation. This happens even when the germline-encoded VH sequence has not mutated. Only a few mutations can convert the germline IGHV1-69 to a full-activity CR6261. The existence of an antibody that can identify a common feature of the influenza virus has numerous evolutionary advantages. Continued research in this area may have a positive impact on the development of HIV, hepatitis C and SARS vaccines.
The information I learnt in the classroom helped me understand the article. For example, I was able to correlate my knowledge on the existing influenza vaccine with the article. I already knew that HA stem has a conserved site which is vulnerable, and that its vulnerability is promising for the use of broadly reactive antibodies. I also knew that the existing influenza vaccine is limited because it bears strain specific antibodies. These antibodies cannot adapt to a variable and immunodominant head. In addition, my knowledge of the common building blocks such as amino-acids helped me understand how proteins are constituted and how anti-bodies work. When the authors refer to terms like soluble immunoglobulin-G (IgG), I know what they mean. Because I know that they are referring to a type of a soluble antibody moves from a cell through the cell membrane (Lingwood et al. 566)
Conclusion
The research by Lingwood et al. examines how influenza haemagglutinin stimulates naïve B cells into maturation and induces protective immunity. This research is important because it can lead to the development of a universal influenza vaccine that is effective even as variants of the influenza virus continue to evolve. According to Lingwood et al. (569), the findings made by this research have numerous evolutionary advantages and may positively affect researches into the development of HIV, hepatitis C and SARS vaccines.
Work Cited
Lingwood, Daniel, Patrick M. Mctamney, Hadi M. Yassine, James R. R. Whittle, Xiaoti Guo, Jeffrey C. Boyington, Chih-Jen Wei, and Gary J. Nabel. "Structural and genetic basis for development of broadly neutralizing influenza antibodies." Nature 489.7417 (2012): 566-570. Print.
