The same cannot be said of interferon non-responsive cancer cells, a quality which allows VSIV to grow and lyse oncogenic cells preferentially.Recently, attenuated VSIV with a mutation in its M protein has been found to have oncolytic properties. Research is ongoing, and has shown VSIV to reduce tumor size and spread in melanoma, lung cancer, colon cancer and certain brain tumors in laboratory models of cancer. Anti-HIV therapy
VSIV was modified to attack HIV-infected T-cells. The modified virus was called a "trojan horse" virus [1]

Ebola vaccine
Recombinant VSIV has undergone phase 1 trials as a vaccine for Ebola virus.Recombinant VSIV expressing the Ebola virus glycoprotein has undergone phase III trials in Africa as a vaccine for Ebola virus disease. The vaccine was shown to be 76-100% effective in preventing Ebola virus disease. (see also rVSV-ZEBOV vaccine) In December 2019, Merck & Co.s rVSV-ZEBOV vaccine Ervebo was approved by the Food and Drug Administration to treat individuals 18 and older. Other Uses
Replication competent rVSV has also been created expressing proteins of Lassa fever and Marburg virus. Other applications
The VSIV G protein is routinely used in biomedical research to pseudotype retroviral and lentiviral vectors, conferring the ability to transduce a broad range of mammalian cell types with genes of interest.The VSIV G protein has also been used in cytological studies of trafficking in the endomembrane system.
Organ-limited amyloidosis is a category of amyloidosis where the distribution can be associated primarily with a single organ. It is contrasted to systemic amyloidosis, and it can be caused by several different types of amyloid.In almost all of the organ-specific pathologies, there is debate as to whether the amyloid plaques are the causal agent of the disease or instead a downstream consequence of a common idiopathic agent. The associated proteins are indicated in parentheses. Neurological amyloid
Alzheimers disease (Aβ 39-43)
Parkinsons disease (alpha-synuclein)
Huntingtons disease (huntingtin protein)
Transmissible spongiform encephalopathies caused by prion protein (PrP) were sometimes classed as amyloidoses, as one of the four pathological features in diseased tissue is the presence of amyloid plaques. These diseases include;
Creutzfeldt–Jakob disease (PrP in cerebrum)
Kuru (diffuse PrP deposits in brain)
Fatal familial insomnia (PrP in thalamus)
Bovine spongiform encephalopathy (PrP in cerebrum of cows)

Cardiovascular amyloid
Cardiac amyloidosis
Senile cardiac amyloidosis-may cause heart failure

Other
Amylin deposition can occur in the pancreas in some cases of type 2 diabetes mellitus
Cerebral amyloid angiopathy

References


== External links ==