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Increased Body Temperature01:25

Increased Body Temperature

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A body temperature above  38°C  (100.4 °F) is known as fever or pyrexia, and a person with fever is termed 'febrile.' Typically, the hypothalamus, a part of the brain that acts as the body's thermostat, regulates body temperature through a thermoregulatory setpoint. It receives signals from cold and warm thermal receptors throughout the body and adjusts the body's temperature accordingly. Fever occurs when this hypothalamic setpoint is altered, usually in...
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Among the three main modes of HGT—transformation, conjugation, and transduction—transduction is unique in that it is mediated by bacteriophages, or bacterial viruses.Transduction occurs in two ways. Generalized transduction occurs during the lytic cycle of a bacteriophage infection. In this process, bacteriophages infect bacterial cells, replicate within them, and ultimately cause cell lysis, releasing newly assembled virions. Occasionally, random fragments of the bacterial genome...
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Methods of reducing fever01:22

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The signs and symptoms of fever include hot and dry skin, flushed face, thirst, muscle aches, anorexia, headache, tachycardia, tachypnea, and fatigue. Elevated body temperature is reduced using two methods: pharmacological and nonpharmacological. Proper identification and treatment of the root cause of a fever is of utmost importance.
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Fever can be triggered by several factors, including infections, nervous system disorders, certain cancers, blood diseases like leukemia, embolism, thrombosis, heatstroke, dehydration, surgical trauma, crushing injuries, and allergic reactions.
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Antibodies, or immunoglobulins, are critical players in the immune system's arsenal against invading pathogens. Produced by B cells and plasma cells, their primary role is to detect and bind to specific antigens, molecules found on the surface of pathogens like bacteria or viruses. Beyond antigen recognition, antibodies perform several vital functions that contribute to immune defense.
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Fever as an evolutionary agent to select immune complexes interfaces.

Vlad Tofan1, Alina Lenghel2, Maristela Martins de Camargo3

  • 1Cantacuzino Military-Medical Research and Development National Institute, Bucharest, Romania.

Immunogenetics
|May 11, 2022
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Summary

Fever may optimize antibody binding by influencing the amino acid composition at pathogen and cancer antigen interfaces. This study reveals evolutionary pressures shaping immune complex formation and antibody recognition.

Keywords:
Binding affinityBinding interfacesFeverImmune complexesmAb

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Area of Science:

  • Immunology
  • Structural Biology
  • Evolutionary Biology

Background:

  • Immune complexes are crucial for pathogen and cancer defense.
  • Fever is known to modulate host immune responses.
  • The structural basis of antibody-antigen interactions modulated by fever is not fully understood.

Purpose of the Study:

  • To analyze protein-protein interfaces in immune complexes involving fever-modulated antigens.
  • To compare these interfaces with those not affected by fever.
  • To identify key residues and parameters governing antibody-antigen binding in the context of fever.

Main Methods:

  • Analysis of protein-protein interfaces from the Protein Data Bank.
  • Focus on immune complexes with viral, bacterial, protozoan, and cancer antigens.
  • Identification of 'hotspots' and assessment of structural, kinetic, and thermodynamic parameters.

Main Results:

  • Detailed distribution of amino acids at pathogen/cancer epitopes and monoclonal antibody paratopes.
  • Identification of highly connected residues ('hotspots') at these interfaces.
  • Assessment of parameters influencing the formation of immune complexes.

Conclusions:

  • Evolutionary pressures likely select for specific amino acid types at protein interfaces.
  • Fever may act as a selective force optimizing antibody binding affinity and specificity.
  • Understanding these interactions can inform therapeutic strategies targeting immune responses.