Influenza A is a viral disease of global dimension, presenting with high morbidity and mortality in annual
epidemics, and in pandemics which are of infrequent occurrence but which have very high attack rates. Influenza vaccines
of the future must be directed toward use of conserved group-specific viral antigens, such as are present in transitional
proteins which are exposed during the fusion of virus to the host cell. Influenza probes revealed a continuing battle for
survival between host and parasite in which the host population updates the specificity of its pool of humoral immunity by
contact with and response to infection with the most recent viruses which possess altered antigenic specificity in their
hemagglutinin (HA) ligand. It is well known that the HA protein is found on the surface of the influenza virus particle and
is responsible for binding to receptors on host cells and initiating infection.
Polymorphonuclear neutrophils (PMN) have been reported to be involved in the initial host response to influenza A virus
(IAV). Early after IAV infection, neutrophils infiltrate the airway probably due to release of chemokines that attract PMN.
Clearly, severe IAV infection is characterized by increased neutrophil influx into the lung or upper respiratory tract.
Carnosine (β-alanyl-L-histidine) and anserine (N-β-alanyl-1-methyl-L-histidine) are found in skeletal muscle of most
vertebrates, including those used for food; for example, 100 g of chicken breast contains 400 mg (17.6 mmol/L) of
carnosine and 1020 mg (33.6 mmol/l) of anserine. Carnosine-stimulated respiratory burst in neutrophils is a universal
biological mechanism of influenza virus destruction. Our own studies revealed previously unappreciated functional effects
of carnosine and related histidine containing compounds as a natural biological prevention and barrier against Influenza
virus infection, expand public understanding of the antiviral properties of imidazole-containing dipeptide based
compounds, and suggest important interactions between neutrophills and carnosine related compounds in the host
response to viruses and bacteria. Carnosine and anserine were also found to reduce apoptosis of human neutrophils. In this
way these histidine-containing compounds can modulate the Influenza virus release from neutrophills and reduce virus
dissemination through the body of the organism.
This review points the ability of therapeutic control of Influenza viral infections associated with modulation by oral nonhydrolized
forms of carnosine and related histidine-containg compounds of PMN apoptosis which may be involved at
least in part in the pathophysiology of the disease in animals and humans.
The data presented in this article, overall, may have implications for global influenza surveillance and planning for
pandemic influenza therapeutic prevention with oral forms of non-hydrolized natural L-carnosine as a suitable alternative
to the conventional vaccination for various flu ailments.