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1.
Clin Neuropharmacol ; 39(6): 329-330, 2016.
Article in English | MEDLINE | ID: mdl-27755133

ABSTRACT

A wide range of etiologies can cause hemifacial spasm (HFS), including infection. In this case report, a 44-year-old woman developed HFS and was explored surgically 7 years later. No abnormalities were found. Afterward, treatment of a surgical wound infection with an oral cephalosporin resulted in a temporary HFS remission that had never occurred previously. This antibiotic experience prompted further workup for an underlying infection, which ultimately led to diagnosis of Lyme disease. Presentation of HFS due to Lyme disease has not been reported. Because its diagnosis can be occult and antibiotic therapy can be both diagnostic and therapeutic, Lyme disease should be a consideration for cases of HFS.


Subject(s)
Anti-Bacterial Agents/therapeutic use , Hemifacial Spasm/etiology , Lyme Disease/complications , Lyme Disease/drug therapy , Adult , Echovirus 6, Human/genetics , Echovirus 6, Human/metabolism , Echovirus 6, Human/pathogenicity , Female , Hemifacial Spasm/drug therapy , Humans
2.
Antiviral Res ; 73(3): 151-60, 2007 Mar.
Article in English | MEDLINE | ID: mdl-17023058

ABSTRACT

Lactoferrin, an 80 kDa bi-globular iron-binding glycoprotein belonging to the transferrin family, is a pleiotropic factor with potent antimicrobial and immunomodulatory activities, present in breast milk, in mucosal secretions, and in the secondary granules of neutrophils. Recently, we have shown that bovine lactoferrin prevents the early phases of echovirus infection and also acts as a survival factor inhibiting viral-induced apoptosis. In the present research we investigated the mechanism of bovine lactoferrin anti-echoviral effect demonstrating that echovirus enters susceptible cells by an endocytic pathway and that lactoferrin treatment is able to prevent viral genome delivery into the cytoplasm. It is likely that lactoferrin interaction with echovirus capsid proteins induces alterations that stabilize the conformation of the virion making it resistant to uncoating. Taken together, the results of our study show that the inhibition of echovirus 6 infectivity by lactoferrin is dependent on its interaction not only with cell surface glycosaminoglycan chains but also with viral structural proteins demonstrating that this glycoprotein targets the virus entry process.


Subject(s)
Echovirus 6, Human/drug effects , Lactoferrin/pharmacology , Viral Structural Proteins/metabolism , Ammonium Chloride/pharmacology , Animals , Cattle , Chlorocebus aethiops , Echovirus 6, Human/metabolism , Echovirus 6, Human/physiology , Echovirus 6, Human/ultrastructure , Endocytosis/physiology , Hydrogen-Ion Concentration , Lactoferrin/metabolism , Virus Attachment/drug effects
3.
Neurol Neurochir Pol ; 40(1): 28-33, 2006.
Article in Polish | MEDLINE | ID: mdl-16463219

ABSTRACT

BACKGROUND AND PURPOSE: The role of viral infection in the pathogenesis of ALS has been raised many times in the previous papers. The presence of an enterovirus genome has previously been confirmed using PCR RT and PCR in situ in spinal cord tissue samples taken from patients who died of ALS. Viral genome sequencing has also been used to show 91% and 88% homogeneity with ECHO 6 and 7 viruses, respectively. A year later the same method did not confirm the presence of the virus in spinal cord fragments taken from 30 patients who died of ALS nor in an 18 person control group. The present study was aimed to find persistent ECHO 6 and 7 viral infections in tissue samples taken from patients who died of ALS. MATERIAL AND METHODS: RNA was isolated from frozen medulla oblongata samples taken from six patients who died of ALS (hospitalized in the Neurological Clinic CSK AM in the years 2000-2002). The presence of RNA was confirmed using RNA beta-actine. Oligo 2 and 3 as well as pEforward and pErevers primers were used for amplification. RESULTS: All samples returned negative results. CONCLUSIONS: In the samples studied no correlation was found between ECHO 6 and 7 viral infections and ALS.


Subject(s)
Amyotrophic Lateral Sclerosis , Enterovirus B, Human/genetics , Enterovirus B, Human/metabolism , Medulla Oblongata/metabolism , Medulla Oblongata/pathology , RNA, Viral/genetics , RNA, Viral/metabolism , Sequence Analysis, RNA/methods , Actins/genetics , Aged , Amyotrophic Lateral Sclerosis/metabolism , Amyotrophic Lateral Sclerosis/mortality , Amyotrophic Lateral Sclerosis/pathology , DNA Primers/genetics , DNA, Complementary/genetics , DNA, Viral/genetics , Echovirus 6, Human/genetics , Echovirus 6, Human/metabolism , Female , Humans , Male , Middle Aged , Reverse Transcriptase Polymerase Chain Reaction
4.
J Gen Virol ; 79 ( Pt 7): 1707-13, 1998 Jul.
Article in English | MEDLINE | ID: mdl-9680134

ABSTRACT

Several echoviruses (EVs) have previously been shown to use decay accelerating factor (DAF) as a cellular receptor. Since DAF is expressed on erythrocytes, EVs that use this receptor cause haemagglutination. Here we show that all EVs that haemagglutinate do so via attachment to DAF and that this interaction can be inhibited by a monoclonal antibody (MAb) specific for DAF domain SCR3. Although the viruses haemagglutinate via DAF some can bind to rhabdomyosarcoma cells from which DAF has been removed and infect in the presence of a MAb against DAF. This suggests that some EVs have the capacity to interact with more than one cellular receptor.


Subject(s)
CD55 Antigens/metabolism , Enterovirus B, Human/metabolism , Receptors, Virus/metabolism , Animals , Antibodies, Monoclonal/metabolism , CD55 Antigens/genetics , CD55 Antigens/immunology , Cell Line , Echovirus 6, Human/metabolism , Hemagglutination , Hemagglutination Inhibition Tests , Humans , Mice , Phosphatidylinositol Diacylglycerol-Lyase , Sulfur Radioisotopes , Tumor Cells, Cultured , Type C Phospholipases/metabolism , Type C Phospholipases/pharmacology
5.
J Virol ; 63(12): 5268-75, 1989 Dec.
Article in English | MEDLINE | ID: mdl-2585604

ABSTRACT

We established a human cell line which was persistently infected (PI) by the normally cytolytic echovirus 6. All of the cultured PI cells contained genome-size viral RNA which was synthesized continuously and incorporated into virus particles. This steady-state infection has been maintained for more than 6 years. In contrast to RNA of wild-type echovirus 6, the viral RNA from PI cells was not lytic when transfected into uninfected, susceptible cells. The capsid polypeptides of the virus particles produced during lytic infections were compared with those of virus particles from PI cells. Wild-type virions contained five polypeptides with molecular masses of 31.5, 27, 25.8, 21.2, and 9.5 kilodaltons. Comparison of polypeptide profiles of virions and empty immature capsids along with peptide analyses by immunoblotting and partial proteolysis of isolated viral proteins identified the cleavage products of the 31.5-kilodalton polypeptide (VP0) as the two smaller polypeptides (VP2 and VP4). The virus particles produced by PI cells as well as cellular extracts of PI cells contained only the three largest proteins (VP0, VP1, and VP3), indicating that VP0 was not processed during persistent infection. The lack of VP2 and VP4 in the defective virus particles coincided with their inability to attach to uninfected, susceptible cells. The maintenance of the steady-state infection of echovirus 6 was not dependent upon the release of virus particles from PI cells.


Subject(s)
Capsid/genetics , Cell Transformation, Viral , Echovirus 6, Human/genetics , Enterovirus B, Human/genetics , RNA, Viral/genetics , Cell Line , DNA Probes , DNA, Viral/genetics , Echovirus 6, Human/metabolism , Electrophoresis, Polyacrylamide Gel , Humans , Nucleic Acid Hybridization , Proteins/isolation & purification , RNA, Messenger/genetics , RNA, Messenger/isolation & purification , RNA, Viral/isolation & purification , Viral Proteins/isolation & purification
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