Parasitic Wasps

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[Katinka]

Originally Posted by Kammy

To complement our studies in vivo, we study viral pathogenesis and virus-host interactions at the cell and molecular levels as well.

These studies primarily are focused on the role of actin, one of the most abundant cellular proteins, in these processes.

Actin appears to be involved in viral movement, nucleocapsid morphogenesis, and regulation of the switch from production of one viral phenotype to the other.

Accordingly, dramatic sequential changes take place in the distribution and quantity of microfilaments throughout the course of infection which correlate with different phases of virus replication.

In uninfected cells, microfilaments appear to be associated primarily with the plasma membrane.

Upon infection, correlated with virus uptake and independent of early virus gene expression, thickened cables of microfilament bundles appear.

Next, dependent upon early virus gene expression, microfilaments appear as ventral aggregates.

Finally, and dependent on late gene expression, microfilaments appear within the nucleus where they co-localize with newly synthesized capsid protein during nucleocapsid assembly."

This is incredible Kam**! Great research btw....It's BIOINSECTICIDE!!

As I read how Actin is involved here it reminded me of my research at the Paper Thread and Silica Thread..This all fits together...

Post # 55 + 162


Actin - Wikipedia, the free encyclopedia

....Actin is a globular, roughly 42-kDa protein found in all eukaryotic cells (the only known exception being nematode sperm) where it may be present at concentrations of over 100 μM. It is also one of the most highly-conserved proteins, differing by no more than 20% in species as diverse as algae and humans.

Actin is the monomeric subunit of two types of filaments in cells: microfilaments, one of the three major components of the cytoskeleton, and thin filaments, part of the contractile apparatus in muscle cells.

Thus, actin participates in many important cellular processes including muscle contraction, cell motility, cell division and cytokinesis, vesicle and organelle movement, cell signaling, and the establishment and maintenance of cell junctions and cell shape. Many of these processes are mediated by extensive and intimate interactions of actin with cellular membranes.
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Microfilaments

Individual subunits of actin are known as globular actin (G-actin). G-actin subunits assemble into long filamentous polymers called F-actin. Two parallel F-actin strands must rotate 166 degrees in order for them to layer correctly on top of each other. This gives the appearance of a double helix and, more importantly, gives rise to microfilaments of the cytoskeleton. Microfilaments measure approximately 7 nm in diameter with a loop of the helix repeating every 37 nm.


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Actomyosin filaments

In muscle, actin is the major component of thin filaments, which, together with the motor protein myosin (which forms thick filaments), are arranged into actomyosin myofibrils.

These fibrils comprise the mechanism of muscle contraction. Using the hydrolysis of ATP for energy, myosin heads undergo a cycle during which they attach to thin filaments, exerting a tension, and then depending on the load, perform a power stroke that causes the thin filaments to slide past, shortening the muscle.

In contractile bundles, the actin-bundling protein alpha-actinin separates each thin filament by ~35 nm. This increase in distance allows thick filaments to fit in between and interact, enabling deformation or contraction.

In deformation, one end of myosin is bound to the plasma membraneactin filament. while the other end "walks" toward the plus end of the

This pulls the membrane into a different shape relative to the cell cortex.

For contraction, the myosin molecule is usually bound to two separate filaments and both ends simultaneously "walk" toward their filament's plus end, sliding the actin filaments closer to each other.

This results in the shortening, or contraction, of the actin bundle (but not the filament). This mechanism is responsible for muscle contraction and cytokinesis, the division of one cell into two.


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Straub continued to work on actin and in 1950 reported that actin contains bound ATP [7] and that, during polymerisation of the protein into microfilaments, the nucleotide is hydrolysed to ADP and inorganic phosphate (which remain bound in the microfilament). Straub suggested that the transformation of ATP-bound actin to ADP-bound actin played a role in muscular contraction. In fact, this is true only in smooth muscle, and was not supported through experimentation until 2001.[8]
The crystal structure of G-actin was solved in 1990 by Kabsch and colleagues.[9] In the same year a model for F-actin was proposed by Holmes and colleagues.[10] The model was derived by fitting a helix of G-actin structures according to low-resolution fiber diffraction data from the filament. Several models of the filament have been proposed since. However there is still no high-resolution X-ray structure of F-actin.

The Listeria bacteria use the cellular machinery to move around inside the host cell, by inducing directed polymerisation of actin by the ActAtransmembrane protein, thus pushing the bacterial cell around.

Kat

[Katinka]

You Tube

[Katinka]

YouTube - actin filament

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[Katinka]

Actin...
Formation of thin filament

[Katinka]

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Actin - Wikipedia, the free encyclopedia


Here Kambo!!

The growth of actin filaments can be regulated by thymosin and profilin.

Thymosin binds to G-actin to prevent it from polymerizing while profilin binds to G-actin to promote monomeric addition to the barbed, plus end.

Let me look up what thymosin and profilin means..hmm..

Kat

[Katinka]

Thymosin

Thymosin - Wikipedia, the free encyclopedia

Thymosin is an actin-binding protein in cells.

It promotes the development of immune-system cells.

The predominant form of thymosin, thymosin β4, is a member of a highly conserved family of actin monomer-sequestering proteins.


β-thymosins are the primary regulators of unpolymerized actin, and are essential for maintaining the small cytoplasmic pool of free G-actin monomers required for rapid filament elongation and allowing for the flux of monomers between the thymosin-bound pool and F-actin (Dedova et al., 2006).



Thymosin β4 sequesters actin, holding it in a form that is unable to polymerize.

Due to its profusion in the cytosol and its ability to bind ATP G-actin but not F-actin, thymosin β4 is regarded as the principal actin-sequestering protein.

Tβ4 binds ATP G- monomeric actin in a 1:1 complex where G-actin cannot polymerize.

Thymosin β4 (Tβ4) functions like a buffer for monomeric actin....

so..the Thymus is involved here....How many Morgies have reported to have thyroid problems too, I'm asking??

The effect of thymosin and profilin on actin polymerization is shown.

When thymosin binds to an actin monomer it sterically prevents further binding to and elongation of the plus end of the actin filament.

In contrast, when profilin binds to an actin monomer the filament is still capable of elongating.

As thymosin and profilin cannot both bind to a single actin monomer at the same time, there is competition between the inhibitory thymosin and the profilin.

Generally a majority of actin monomer is thymosin-bound, thus the activation of a small amount of profilin produces rapid filament assembly.

Profilin binds to actin monomers that are temporarily released from the thymosin-bound monomer pool, shuttles them onto the plus ends of actin filaments, and is then released and recycled for further rounds of filament elongation.

Therefore, the polymerization of actin is controlled by the give and take between thymosin and profilin.

Here it is:

Skin is the largest organ of the body, which makes up 16% of total body weight.

It is also the largest organ that provides immune protection and plays a role in inflammation.

Composed of specialized epithelial and connective tissue cells, skin is our major interface with the environment, a shield from the outside world and a means of interacting with it.

As such, the skin is subjected to insults and injuries: burns from the sun’s ultraviolet radiation that elicit inflammatory reactions, damage from environmental pollutants and wear and tear that comes with aging.

Thymosin beta 4 accelerated skin wound healing in a rat model of a full thickness wound where the epithelial layer was destroyed.

When Tb4 was applied topically to the wound or injected into the animal, epithelial layer restoration in the wound was increased 42% by day four and 61% by day seven, after treatment, compared to untreated.

Tb4 stimulated collagen deposition in the wound and angiogenesis.

Tb4 accelerated keratinocyte migration, resulting in the wound contracting by more than 11%, compared to untreated wounds, to close the skin gap in the wound.

An analysis of skin sections (histological observations) showed that the Tb4 treated wounds healed faster than the untreated.

Proof of accelerated cell migration was also seen in vitro, where Tb4 increased keratinocyte migration two to threefold, within four to five hours after treatment, compared to untreated keratinocytes.

A critical step in wound healing is angiogenesis.

New vessels are needed to supply nutrients and oxygen to the cells involved in repair, to remove toxic materials and debris of dead cells and generate optimal conditions for new tissue formation.

Another important step is the directional migration of cells into the injured area, joining up to repair the wound.

This requires an attractant that will direct the cells to the wound and propel them to the site.

From what I understand.... Morgellons Disease and the possibility to be infected is related to malfunction or dysfunction of the Endocrine Glands and it's production of hormones?

Kat