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   TID: hpt/lnx 1.9.0-cur 2019-01-08   
    Fintetuning for antibodies    
    The strength of the immune reaction triggered by antibodies can be   
   regulated    
      
     Date:   
         July 14, 2023   
     Source:   
         Friedrich-Alexander-Universita"t Erlangen-Nu"rnberg   
     Summary:   
         Antibodies are crucial, not only for treating tumors and infections.   
      
         Sometimes, however, the immune reaction they trigger can be too   
         strong and end up causing more damage, for example in the case of   
         people infected with Covid-19. Problems such as these can often   
         be avoided by finetuning antibodies, according to new research.   
      
      
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   Antibodies are crucial, not only for treating tumors and   
   infections. Sometimes, however, the immune reaction they trigger can   
   be too strong and end up causing more damage, for example in the case   
   of people infected with Covid-19. Problems such as these can often be   
   avoided by finetuning antibodies, as Prof. Dr. Falk Nimmerjahn from   
   Friedrich-Alexander-Universita"t Erlangen-Nu"rnberg (FAU) and two of   
   his colleagues in the Netherlands and in the UK have now reported in   
   thejournal_Nature_Immunology.   
      
   In his laboratories, the FAU researcher is carrying out research into   
   immunoglobulin G, or IgG in short, that provides long-lasting protection   
   against infection in the bodies of humans and animals. These biomolecules   
   that are often used in modern medicine consist of two long and two short   
   chains of proteins that link together to form a Y-shaped structure. For   
   many years, research and medicine has focused on the two top branches of   
   this Y for good reason: the two ends form a type of pocket which smaller   
   structures on the surface of bacteria and other pathogens fit into,   
   similarly to a key in a lock.   
      
   Key-lock principle in immune system Just like a locksmith can produce   
   very many different locks and the matching keys by only making a few   
   slight changes, the immune system also produces very many different   
   structures at the ends of immunoglobulins that match to very many   
   different pathogens. After an infection with a specific bacterium or   
   virus, these IgG created during the immune reaction remain on patrol   
   within the body for a very long time and can react extremely rapidly in   
   the case of a renewed infection.   
      
   If the key fits the lock, the immunoglobulin attaches to the pathogen   
   and marks it for other immune specialists within the immune system. The   
   antibody serves to mark tumor cells or pathogens to make them stand   
   out from the huge quantities of cells and harmless microorganisms that   
   circulate throughout the body and take on important functions in the   
   bodies of humans and animals.   
      
   Using genetic glue to fight bacteria Once this stage has been   
   successfully completed, this is when the backbone of the Y-shaped   
   IgG comes into play. It is this backbone that Falk Nimmerjahn is now   
   investigating closely at his Chair of Genetics. Macrophages, killer   
   cells and granulocytes take over in the end phase of the battle against   
   an infection.   
      
   "We have often observed cells working as a team, with granulocytes   
   taking on a suicidal role;" Falk Nimmerjahn explains. Attracted by the   
   antibody that has found its target, these cells burst, releasing their   
   relatively sticky genetic material from their core. The bacteria that   
   the IgG previously identified as being harmful stick to this matter.   
      
   These microorganisms can be extremely dangerous, but have now been   
   rendered helpless, and are easy prey for the macrophages that have also   
   been attracted and can now consume the bacteria that the antibodies   
   have tracked down and marked. However, the macrophages are often rather   
   aggressive and act with little consideration of possible consequences. If   
   time is running out in the race between life and death, collateral damage   
   is accepted as being unavoidable, and substances such as oxygen radicals   
   and other dangerous products that would normally be rendered harmless are   
   released. For most patients this is of no consequence: The main priority   
   is survival, any resulting damage should be able to be repaired later.   
      
   One of the factors modulating the immune reaction involves small   
   posttranslational modifications that are made to the backbone of the   
   immunoglobulin after the antibody has been created. This involves,   
   for example, little sugar molecules that are attached to the backbone   
   of the immunoglobulin.   
      
   They seem to play a crucial role in the finetuning of the immune   
   reaction. "If the right components are missing, it makes the immune   
   reaction much more severe," explains Falk Nimmerjahn.   
      
   That can, however, have fatal consequences, for example if a viral   
   infection has already severely damaged tissue. If the control mechanism   
   on the backbone of the immunoglobulin is adjusted to only attach a little   
   sugar and therefore induce a strong reaction, that may cause dangerously   
   severe damage to an organ that is already stretched to its limit, such as   
   the lung in the event of a viral infection. According to Falk Nimmerjahn,   
   "the organism therefore adjusts its control mechanisms very exactly." In   
   cases such as this, the control mechanisms are set to trigger a weak   
   reaction with many chains of sugar.   
      
   Gaining an exact knowledge of this antibody tuning within the context   
   of an immune response is fundamental if we are to improve and increase   
   patients' tolerance of antibodies used to treat tumors and autoimmune   
   diseases.   
      
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   Materials provided by Friedrich-Alexander-Universita"t_Erlangen-Nu"rnberg.   
      
   Note: Content may be edited for style and length.   
      
      
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   Journal Reference:   
      1. Falk Nimmerjahn, Gestur Vidarsson, Mark S. Cragg. Effect of   
         posttranslational modifications and subclass on IgG activity:   
         from immunity to immunotherapy. Nature Immunology, 2023; DOI:   
         10.1038/s41590- 023-01544-8   
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   Link to news story:   
   https://www.sciencedaily.com/releases/2023/07/230714114736.htm   
      
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