scholarly journals A mouse monoclonal antibody against influenza C virus attenuates acetaminophen-induced liver injury in mice

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Yutaka Sasaki ◽  
Naoto Yoshino ◽  
Takako Okuwa ◽  
Takashi Odagiri ◽  
Takashi Satoh ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Serum Level ◽  
Hepatic Injury ◽  
Molecular Mimicry ◽  
Host Proteins ◽  
Serum Alanine Aminotransferase ◽  
Therapeutic Function ◽  
Fusion Glycoprotein ◽  
Influenza C Virus ◽  
Alt Activity

AbstractMolecular mimicry is one of the main processes for producing autoantibodies during infections. Although some autoantibodies are associated with autoimmune diseases, the functions of many autoantibodies remain unknown. Previously, we reported that S16, a mouse (BALB/c) monoclonal antibody against the hemagglutinin-esterase fusion glycoprotein of influenza C virus, recognizes host proteins in some species of animals, but we could not succeed in identifying the proteins. In the present study, we found that S16 cross-reacted with acetyl-CoA acyltransferase 2 (ACAA2), which is expressed in the livers of BALB/c mice. ACAA2 was released into the serum after acetaminophen (APAP) administration, and its serum level correlated with serum alanine aminotransferase (ALT) activity. Furthermore, we observed that S16 injected into mice with APAP-induced hepatic injury prompted the formation of an immune complex between S16 and ACAA2 in the serum. The levels of serum ALT (p < 0.01) and necrotic areas in the liver (p < 0.01) were reduced in the S16-injected mice. These results suggest that S16 may have a mitigation function in response to APAP-induced hepatotoxicity. This study shows the therapeutic function of an autoantibody and suggests that an antibody against extracellular ACAA2 might be a candidate for treating APAP-induced hepatic injury.

The epitope sequence of S16, a monoclonal antibody against influenza C virus hemagglutinin-esterase fusion glycoprotein

2017 ◽  
Vol 12 (3) ◽  
pp. 93-101
Author(s):  
Takako Okuwa ◽  
Yutaka Sasaki ◽  
Yoko Matsuzaki ◽  
Toshiki Himeda ◽  
Naoto Yoshino ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Epitope Sequence ◽  
Fusion Glycoprotein ◽  
Influenza C Virus

scholarly journals Influenza Virus Assembly and Lipid Raft Microdomains: a Role for the Cytoplasmic Tails of the Spike Glycoproteins

2000 ◽  
Vol 74 (10) ◽  
pp. 4634-4644 ◽  
Author(s):  
Jie Zhang ◽  
Andrew Pekosz ◽  
Robert A. Lamb
Keyword(s):  
Influenza Virus ◽  
Influenza A ◽  
Virus Assembly ◽  
Intrinsic Property ◽  
Influenza Viruses ◽  
Apical Surface ◽  
Cytoplasmic Tails ◽  
Fusion Glycoprotein ◽  
Influenza C Virus ◽  
Lipid Raft Microdomains

ABSTRACT Influenza viruses encoding hemagglutinin (HA) and neuraminidase (NA) glycoproteins with deletions in one or both cytoplasmic tails (HAt− or NAt−) have a reduced association with detergent-insoluble glycolipids (DIGs). Mutations which eliminated various combinations of the three palmitoylation sites in HA exhibited reduced amounts of DIG-associated HA in virus-infected cells. The influenza virus matrix (M1) protein was also found to be associated with DIGs, but this association was decreased in cells infected with HAt− or NAt− virus. Regardless of the amount of DIG-associated protein, the HA and NA glycoproteins were targeted primarily to the apical surface of virus-infected, polarized cells. The uncoupling of DIG association and apical transport was augmented by the observation that the influenza A virus M2 protein as well as the influenza C virus HA-esterase-fusion glycoprotein were not associated with DIGs but were apically targeted. The reduced DIG association of HAt− and NAt− is an intrinsic property of the glycoproteins, as similar reductions in DIG association were observed when the proteins were expressed from cDNA. Examination of purified virions indicated reduced amounts of DIG-associated lipids in the envelope of HAt− and NAt− viruses. The data indicate that deletion of both the HA and NA cytoplasmic tails results in reduced DIG association and changes in both virus polypeptide and lipid composition.

Correlation between the Presence of Natural Antitumor Antibodies and Activation of Mulv Endogenous Virus in Balb/C Mice

1981 ◽  
Vol 67 (4) ◽  
pp. 283-292 ◽  
Author(s):  
Sylvie Ménard ◽  
Maria I. Colnaghi ◽  
Elda Tagliabile
Keyword(s):  
Monoclonal Antibody ◽  
T Cells ◽  
Serum Level ◽  
Tumor Cells ◽  
Cytotoxic Effect ◽  
Spleen Cells ◽  
Endogenous Virus ◽  
Cell Compartment ◽  
Cytotoxic Antibodies ◽  
Antitumor Antibodies

Individual 3-month-old or 12-month-old BALB/c mice, as well as 5-month-old nu/nu or nu/ + BALB/c mice, showed a direct correlation between the serum level of natural antitumor cytotoxic antibodies and the capacity of spleen cells to infect SC-1 cells permissive for murine ecotropic viruses. Pooled or individual sera from 3-month-old BALB/c mice, negative for the presence of natural antitumor cytotoxic antibodies and whose spleen cells were unable to infect the SC-1 cells, were negative both for SC-1 cells and SC-1 cells infected by MuLV. On the contrary, pooled or individual sera from 15-month-old BALB/c mice, positive for the presence of natural antitumor antibodies and with infecting spleen cells, were cytotoxic for infected SC-1 cells but not for the uninfected ones. The infection of SC-1 cells by MuLV could be inhibited by 3-month-old spleen cells, and this effect was suppressed by depriving the inhibiting spleen cells of T cells by means of an anti-Thy-1 antibody plus complement. The cells with infectious capacity did not belong to the T-cell compartment, as demonstrated by the lack of infection after passing the infecting spleen cells through an anti-Ig column, whereas T-deprivation did not modify the infectious capacity. A natural anti-gp70 monoclonal antibody, which exerted a complement-dependent cytotoxic effect on tumor cells, stronghly inhibited the infection of the permissive SC-1 cells by MuLV.

scholarly journals SARS-CoV-2 selectively mimics a cleavable peptide of human ENaC in a strategic hijack of host proteolytic machinery

2020 ◽  
Author(s):  
Praveen Anand ◽  
Arjun Puranik ◽  
Murali Aravamudan ◽  
AJ Venkatakrishnan ◽  
Venky Soundararajan
Keyword(s):  
Cleavage Site ◽  
Molecular Mimicry ◽  
Immune Surveillance ◽  
Cell Types ◽  
Evolutionary Strategy ◽  
Host Proteins ◽  
Α Subunit ◽  
Putative Receptor ◽  
Acid Cleavage ◽  
Cleavable Peptide

Molecular mimicry of host proteins is an evolutionary strategy adopted by viruses to evade immune surveillance and exploit host cell systems. We report that SARS-CoV-2 has evolved a unique S1/S2 cleavage site (RRARSVAS), absent in any previous coronavirus sequenced, that results in mimicry of an identical FURIN-cleavable peptide on the human epithelial sodium channel α-subunit (ENaC-α). Genetic truncation at this ENaC-α cleavage site causes aldosterone dysregulation in patients, highlighting the functional importance of the mimicked SARS-CoV-2 peptide. Single cell RNA-seq from 65 studies shows significant overlap between the expression of ENaC-α and ACE2, the putative receptor for the virus, in cell types linked to the cardiovascular-renal-pulmonary pathophysiology of COVID-19. Triangulating this cellular fingerprint with amino acid cleavage signatures of 178 human proteases shows the potential for tissue-specific proteolytic degeneracy wired into the SARS-CoV-2 lifecycle. We extrapolate that the evolution of SARS-CoV-2 into a global coronavirus pandemic may be in part due to its targeted mimicry of human ENaC and hijack of the associated host proteolytic network.

scholarly journals X-ray crystallographic determination of the structure of the influenza C virus haemagglutinin-esterase-fusion glycoprotein

1999 ◽  
Vol 55 (5) ◽  
pp. 945-961 ◽  
Author(s):  
Xiaodong Zhang ◽  
Peter B. Rosenthal ◽  
Frank Formanowski ◽  
Wolfgang Fitz ◽  
Chi-Huey Wong ◽  
...  
Keyword(s):  
X Ray ◽  
Fusion Glycoprotein ◽  
Influenza C Virus ◽  
Virus Haemagglutinin

scholarly journals Cryo-EM Structure of Nipah Virus Fusion Glycoprotein in Complex with a Monoclonal Antibody Reveals Mechanism of Neutralization

2019 ◽  
Vol 25 (S2) ◽  
pp. 1328-1329
Author(s):  
Ha V. Dang ◽  
Yee-Peng Chan ◽  
Young-Jun Park ◽  
Christopher C. Broder ◽  
David Veesler
Keyword(s):  
Monoclonal Antibody ◽  
Nipah Virus ◽  
Virus Fusion ◽  
Fusion Glycoprotein

Incidence of Hepatotoxicity in Iranian Patients With HIV on Antiretroviral Therapies and Its Correlation with Virologic Response to HIV Treatment

2020 ◽  
Author(s):  
Tayebeh Hashempour ◽  
Javad Moayedi ◽  
Zahra Mousavi ◽  
Masoumeh Esmaeli ◽  
Azizeh Asadzadeh ◽  
...  
Keyword(s):  
Virologic Response ◽  
Hiv Treatment ◽  
Hiv Viral Load ◽  
Serum Alanine Aminotransferase ◽  
Severe Hepatotoxicity ◽  
Antiretroviral Therapies ◽  
Significant Difference ◽  
Periodic Monitoring ◽  
Iranian Patients ◽  
Alt Activity

Abstract Objective To investigate hepatotoxicity in Iranian patients with HIV to assess the association between virologic response to HIV treatment and serum alanine aminotransferase (ALT). Methods This study was conducted with 200 control patients, 75 patients with HIV naïve to antiretroviral therapy (ART), and 443 patients who received ARTs with virologic response (≤1000 copies/mL) or virologic treatment failure (&gt;1000 copies/mL). Serum ALT level and HIV viral load were determined in all patients. Results Patient ALT levels were significantly higher than those of control patients (45.1 ± 44.4 IU/L vs 23.8 ± 5.4 IU/L). Compared to patients who were ART-naïve, patients with ART experience had significantly higher ALT levels (38.2 ± 26.2 IU/L vs 46.3 ± 46.7 IU/L), and severe hepatotoxicity was only detected in those with ART experience (8 patients, 1.8%). Mean ALT had no significant difference between virologic response/failure groups. The ALT activity and HIV load had a negative correlation coefficient, but it was not significant. Conclusion Periodic monitoring for the possibility of hepatotoxicity is highly recommended in all patients with HIV, especially in those receiving ART treatment.

scholarly journals PROTECTIVE EFFECT OF CURCUMIN RIMPANG CURCUMA LONGA LINN. EXTRACT ON CHLORPYRIFOS POISONING IN WISTAR RATS

2021 ◽  
Vol 21 (2) ◽  
Author(s):  
Azhari Muslim ◽  
Dadang Muslim ◽  
Nastiti Siswi Indrasti ◽  
Yusman Syaukat
Keyword(s):  
Protective Effect ◽  
Confidence Level ◽  
Wistar Rats ◽  
Curcuma Longa ◽  
R Software ◽  
Serum Alanine Aminotransferase ◽  
Factorial Anova ◽  
Randomized Design ◽  
Multiple Comparison Test ◽  
Alt Activity

This study used an experimental method in the laboratory with a randomized design with five treatments and six repetitions. The parameters examined were cholinesterase (ChE), Aspartate Aminotransferase (AST), and serum Alanine Aminotransferase (ALT) of blood in the first and second treatment stages. Data were analyzed using factorial ANOVA test and LSD multiple comparison test with 95% confidence level with R software version 3.6.2. Wistar rats were given chlorpyrifos (6.75, 13.5, 27, 54) mg/kg BW/day orally once a day for 28 consecutive days, then further intervention with curcumin (27, 54, 108 and 216) mg/kg BW/day once a day for 14 consecutive days. A significant increase in ChE activity and a significant decrease in AST and ALT activity. This study shows that curcumin from Curcuma longa Linn rhizome extract provides a protective effect against chlorpyrifos poisoning in Wistar rats.

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