Formation of Actin Filaments in Mammalian Cells – Baculovirus Protein FALPE and p10

FALPE and p10 Insect virus protein embedded in the Baculovirus might cause the proliferating formation of Actin Protein Filaments in humans bodies..mainly Morgellons Sufferers.

As we know, the so called ‘fibers’ are seen to be the main symptom of this disease. 100% have reported to have them in/on lesions or have them emerging from intact skin or hair follicles.

I believe that the infectious Baculovirus leads to an over reaction of Actin Protein filament production in our organism due to influence of the Insect virus proteins FALPE and p10.

Here are a few excerpts out of the explanation of Actin Protein Filaments:

Actin is a globular, roughly 42-kDa protein found in all eukaryotic cells.

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.

Principal interactions of structural proteins are at cadherin-based adherens junction. Actin filaments are linked to α-actinin and to the membrane through vinculin. The head domain of vinculin associates to E-cadherin via α-, β-, and γ-catenins. The tail domain of vinculin binds to membrane lipids and to actin filaments.

The protein actin is one of the most highly conserved throughout evolution because it interacts with a large number of other proteins.

All non-spherical prokaryotes appear to possess genes such as MreB, which encode homologues of actin; these genes are required for the cell’s shape to be maintained. The plasmid-derived gene ParM encodes an actin-like protein whose polymerised form is dynamically unstable, and appears to partition the plasmid DNA into the daughter cells during cell division by a mechanism analogous to that employed by microtubules in eukaryotic mitosis.

Actin has four main functions in cells :

  • To form the most dynamic one of the three subclasses of the cytoskeleton, which gives mechanical support to cells, and hardwires the cytoplasm with the surroundings to support signal transduction.
  • To allow cell motility (see Actoclampin molecular motors), including phagocytosis of bacteria by macrophages.
  • In muscle cells to be the scaffold on which myosin proteins generate force to support muscle contraction.
  • In non-muscle cells as a track for cargo transport myosins [non-conventional myosins] such as myosin V and VI. Non-conventional myosins transport cargo, such as vesicles and organelles, in a directed fashion, using ATP hydrolysis, at a rate much faster than diffusion. Myosin V walks towards the barbed end of actin filaments, while myosin VI walks toward the pointed end. Most actin filaments are arranged with the barbed end toward the cellular membrane and the pointed end toward the cellular interior. This arrangement allows myosin V to be an effective motor for export of cargos, and myosin VI to be an effective motor for import.

Pathway of Baculovirus in mammalian cells

We have studied the infection pathway of Autographa californica multinuclear polyhedrosis virus (baculovirus) in mammalian cells.

By titration with a baculovirus containing a green fluorescent protein cassette, we found that several, but not all, mammalian cell types can be infected efficiently.

We demonstrate for the first time that this baculovirus can infect nondividing mammalian cells, which implies that the baculovirus is able to transport its genome across the nuclear membrane of mammalian cells.

Our data further show that the virus enters via endocytosis, followed by an acid-induced fusion event, which releases the nucleocapsid into the cytoplasm.

Cytochalasin D strongly reduces the infection efficiency but not the delivery of nucleocapsids to the cytoplasm, suggesting involvement of actin filaments in cytoplasmic transport of the capsids.

In one study, nucleocapsids of a related baculovirus species (Ploidia interpunctella granulosis virus) were observed docking at the nuclear pore of infected insect cells, at different stages of releasing their genome, but not inside the nucleus.

This suggests a mechanism of DNA transport similar to HSV.

We show here that baculovirus can indeed infect nondividing mammalian cells through a mechanism apparently identical to that found in insect cells.

The mode of nuclear entry of the viral genome appears to be different from what is known of other large DNA viruses.

Our data suggest that the cigar-shaped nucleocapsid (25 nm in diameter) is transported through the nuclear pore, together with the viral genome.




~ by k&k on September 12, 2009.

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