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Ozone in
Air
Ozone can be used to destroy airborne bacteria and eliminate
odours. Ozone kills micro-organisms by a process of oxidation.
Gaseous Ozone can reduce the ammonia concentrations in animal
sheds.
There are two methods that can be used to treat poultry sheds.
When sheds are empty of birds and the litter cleared, high
concentrations of ozone can be used to sanitise the building.
Then using low level concentrations of ozone during the growth
cycle will improve animal hygiene by reducing odorous compounds
present in the growing shed.
Ozone in
water
Highly ozonated water is of enormous benefit in the
slaughterhouse for bacteria control of dead animals and the
environment. When chilled ozonated water is sprayed onto chicken
meat it will kill pathogens on the surface reducing the
potential for spoilage. Slaughterhouse and equipment can also be
washed with highly ozonated water acting to disinfect the
working area reducing the potential for dangerous bacteria
outbreak.
Influenza is a recurrent global disease with, in pandemic
conditions, significant morbidity and lethality. The dynamics of
avian influenza are complicated by the fact that its virus is
capable of evolving in a variety of animal and human reservoirs.
Able to infect all members of the human population in its
pandemic phase, influenza presents supremely challenging
problems in light of its pathogenic capacity and mutational
potential.
Recent advances in immunology have clarified some of the complex
mechanisms of antigen-antibody reactions. This paper explores
two main gases that, produced at the molecular level by cellular
elements of the immune system, perform crucial roles in
microorganism inactivation. The idea that gases are produced in
vivo to perform a panoply of essential biological functions has,
in the last few years, revolutionized concepts about cellular
signaling.
These two physiological gases are nitric oxide and ozone.
Suggested is that, in view of the characteristics inherent in
avian flu, research into the dynamics of these virucidal agents
could assist in the public health response to an influenza
plague.
The Avian influenza virus: Virion architecture and molecular
biology The influenza virus belongs to the small family of
Orthomyxoviruses. Myxo refers to the Greek term
for mucous and this family’s propensity for attachment to the
mucoproteins on cell surfaces. In the case of Avian influenza,
the target cells are the columnar epithelium of the respiratory
tree. The family includes Influenza A, the cause of pandemics,
distinguished by its antigenic surface components. Influenza B,
a milder disease, does not cause pandemics. Influenza C has a
somewhat different genetic structure, infects children and Asian
swine, and causes even milder pathology.
The
avian influenza virion, 100 to 200 nm in diameter is
approximately spherical because of its loose-fitting envelope.
Under the electron microscope it appears as an ovoid organism
studded with hundreds of spikes, the peplomers. If it were
expanded, it would look like a sea urchin. Within the viral core
are eight separate helical single strands of ribonucleoprotein,
the software for viral life and replication. This unusual
segmented RNA genome encodes the transcription of all viral
components, including structural proteins, enzymes, and lipids.
An intricate membrane, the envelope, surrounds the viral genome.
Matrix proteins provide internal attachment between the genomic
nucleocapsid and its envelope. The Avian influenza envelope has
an inner protein (M) shell covered by another shell composed of
a double layer of lipids. Approximately 60% of envelope lipids
are composed of phospholipids and the rest are cholesterols.
Embedded in the envelope are the roots of the peplomers.
Peplomer spikes are essential for viral attachment and
penetration into host cells. Peplomers are constructed of
carbohydrate and protein components, glycoproteins. Of the
several hundred peplomers studding an individual influenza
virion, 80% are the triangular-shaped hemaglutinin (HA)
glycoproteins, and the rest are the mushroom-shaped
neuraminidase (NA) glycoproteins.
HA and NA are vital for avian flu’s infectious capacity. With
regard to the host, HA and NA are the inimical antigens prodding
its immune system’s counter-offensiveness. The hemaglutinin HA
glycoprotein is able to coalesce the red blood cells of a number
of animal species, hence its name. The neuraminidase (NA)
glycoprotein functions as an enzyme, facilitating virus to host
cell attachment and viral release from cells. NA has the
capacity to destroy a component of the host cell surface,
neuraminic acid. The signature proteinic composition of HA and
NA determines the virulence of influenza’s thrust into host
cells. Since 1971, influenza A viruses have been named according
to their HA and NA glycoprotein antigenic compositions. Thus,
the influenza H5N1 strain describes the molecular architecture
of its peplomers. |
