Immunogenicity of synthetic peptides related to the core peptide sequence encoded by the human MUC1 mucin gene: Effect of immunization on the growth of murine mammary adenocarcinoma cells transfected with the human MUC1 gene

1993 ◽  
Vol 36 (1) ◽  
pp. 9-17 ◽  
Author(s):  
Lei Ding ◽  
El-Nasir Lalani ◽  
Mark Reddish ◽  
Rao Koganty ◽  
Ting Wong ◽  
...  
Keyword(s):  
Synthetic Peptides ◽  
Peptide Sequence ◽  
Mammary Adenocarcinoma ◽  
Gene Effect ◽  
The Core ◽  
Mucin Gene ◽  
Muc1 Mucin ◽  
Adenocarcinoma Cells ◽  
Human Muc1 ◽  
Core Peptide

scholarly journals Restricted Isotypic Antibody Reactivity to Hepatitis C Virus Synthetic Peptides in Immunocompromised Patients

1999 ◽  
Vol 6 (2) ◽  
pp. 279-281 ◽  
Author(s):  
Marisol Devesa ◽  
Arlette de Saez ◽  
Graciela León ◽  
Firelei Sirit ◽  
Clarisa Cosson ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Enzyme Immunoassay ◽  
Synthetic Peptides ◽  
Immunocompromised Patients ◽  
The Core ◽  
Antibody Reactivity ◽  
Antibody Isotypes ◽  
Immune Impairment ◽  
Core Peptide

ABSTRACT An enzyme immunoassay based on three synthetic peptides from the core, NS4, and NS5 regions of hepatitis C virus allowed the detection of antibodies in 100% of immunocompetent infected patients and in 91% of immunocompromised patients (hemodialysis and hemophiliac patients). Immune impairment seemed to restrict the spectrum of antibody isotypes reacting to the core peptide.

scholarly journals Biosynthesis and Transport of the Lantibiotic Mutacin 1140 Produced by Streptococcus mutans

2015 ◽  
Vol 197 (7) ◽  
pp. 1173-1184 ◽  
Author(s):  
Jerome Escano ◽  
Byron Stauffer ◽  
Jacob Brennan ◽  
Monica Bullock ◽  
Leif Smith
Keyword(s):  
Streptococcus Mutans ◽  
Posttranslational Modifications ◽  
Cleavage Site ◽  
Peptide Sequence ◽  
Leader Peptide ◽  
Peptide Antibiotics ◽  
The Core ◽  
Core Peptide ◽  
Mutacin 1140 ◽  
Secondary Cleavage

ABSTRACTLantibiotics are ribosomally synthesized peptide antibiotics composed of an N-terminal leader peptide that is cleaved to yield the active antibacterial peptide. Significant advancements in molecular tools that promote the study of lantibiotic biosynthesis can be used inStreptococcus mutans. Herein, we further our understanding of leader peptide sequence and core peptide structural requirements for the biosynthesis and transport of the lantibiotic mutacin 1140. Our study on mutacin 1140 biosynthesis shows a dedicated secondary cleavage site within the leader peptide and the dependency of transport on core peptide posttranslational modifications (PTMs). The secondary cleavage site on the leader peptide is found at the −9 position, and secondary cleavage occurs before the core peptide is transported out of the cell. The coordinated cleavage at the −9 position was absent in alanTdeletion strain, suggesting that the core peptide interaction with the LanT transporter enables uniform cleavage at the −9 position. Following transport, the LanP protease was found to be tolerant to a wide variety of amino acid substitutions at the primary leader peptide cleavage site, with the exception of arginine at the −1 position. Several leader and core peptide mutations produced core peptide variants that had intermediate stages of PTM enzyme modifications, supporting the concept that PTM enzyme modifications, secondary cleavage, and transport are occurring in a highly coordinated fashion.IMPORTANCEMutacin 1140 belongs to the class I lantibiotic family of ribosomally synthesized and posttranslationally modified peptides (RiPPs). The biosynthesis of mutacin 1140 is a highly efficient process which does not lead to a discernible level of production of partially modified core peptide variants. The products isolated from an extensive mutagenesis study on the leader and core peptides of mutacin 1140 show that the posttranslational modifications (PTMs) on the core peptide occur under a highly coordinated dynamic process. PTMs are dictated by the distance of the core peptide modifiable residues from PTM enzyme active sites. The formation of lanthionine rings aids in the formation of successive PTMs, as was observed in a peptide variant lacking a C-terminal decarboxylation.

MZF-1 and DbpA interact with DNase I hypersensitive sites that correlate with expression of the human MUC1 mucin gene

2005 ◽  
Vol 308 (1) ◽  
pp. 41-52 ◽  
Author(s):  
Toshiyuki Shiraga ◽  
John P. Winpenny ◽  
Emma J. Carter ◽  
Victoria A. McCarthy ◽  
Michael A. Hollingsworth ◽  
...  
Keyword(s):  
Dnase I ◽  
Dnase I Hypersensitive Sites ◽  
Mucin Gene ◽  
Muc1 Mucin ◽  
Hypersensitive Sites ◽  
Human Muc1

scholarly journals A plant endophyte Staphylococcus hominis strain MBL_AB63 produces a novel lantibiotic, homicorcin and a position one variant

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
M. Aftab Uddin ◽  
Shammi Akter ◽  
Mahbuba Ferdous ◽  
Badrul Haidar ◽  
Al Amin ◽  
...  
Keyword(s):  
Gene Clusters ◽  
Antimicrobial Activities ◽  
Whole Genome Sequence ◽  
Antimicrobial Substances ◽  
The Core ◽  
Rp Hplc ◽  
Ring Structures ◽  
Core Peptide ◽  
Staphylococcus Hominis ◽  
Epilancin 15X

AbstractHere we report a jute endophyte Staphylococcus hominis strain MBL_AB63 isolated from jute seeds which showed promising antimicrobial activity against Staphylococcus aureus SG511 when screening for antimicrobial substances. The whole genome sequence of this strain, annotated using BAGEL4 and antiSMASH 5.0 to predict the gene clusters for antimicrobial substances identified a novel antimicrobial peptide cluster that belongs to the class I lantibiotic group. The predicted lantibiotic (homicorcin) was found to be 82% similar to a reported peptide epicidin 280 having a difference of seven amino acids at several positions of the core peptide. Two distinct peaks obtained at close retention times from a RP-HPLC purified fraction have comparable antimicrobial activities and LC–MS revealed the molecular mass of these peaks to be 3046.5 and 3043.2 Da. The presence of an oxidoreductase (homO) similar to that of epicidin 280- associated eciO or epilancin 15X- associated elxO in the homicorcin gene cluster is predicted to be responsible for the reduction of the first dehydrated residue dehydroalanine (Dha) to 2-hydroxypropionate that causes an increase of 3 Da mass of homicorcin 1. Trypsin digestion of the core peptide and its variant followed by ESI–MS analysis suggests the presence of three ring structures, one in the N-terminal and other two interlocking rings at the C-terminal region that remain undigested. Homicorcin exerts bactericidal activity against susceptible cells by disrupting the integrity of the cytoplasmic membrane through pore formation as observed under FE-SEM.

Aberrant expression of pyloric gland-type mucin in mucin-producing bile duct carcinomas: A clear difference between the core peptide and the carbohydrate moiety

2005 ◽  
Vol 55 (8) ◽  
pp. 464-470 ◽  
Author(s):  
Masamichi Goto ◽  
Hiroaki Shibahara ◽  
Shugo Tamada ◽  
Tomofumi Hamada ◽  
Koji Oda ◽  
...  
Keyword(s):  
Bile Duct ◽  
Carbohydrate Moiety ◽  
Pyloric Gland ◽  
Aberrant Expression ◽  
The Core ◽  
Core Peptide ◽  
Gland Type

Construction and characterization of a chimeric receptor containing the cytoplasmic domain of MUC1 mucin

2000 ◽  
Vol 278 (3) ◽  
pp. L625-L629 ◽  
Author(s):  
Daoud Meerzaman ◽  
P. X. Xing ◽  
K. Chul Kim
Keyword(s):  
Plasmid Vector ◽  
Cytoplasmic Domain ◽  
Chimeric Receptor ◽  
Signaling Mechanism ◽  
Muc1 Mucin ◽  
Transmembrane Glycoprotein ◽  
Human Muc1 ◽  
Immunologic Assays

MUC1 mucin is a transmembrane glycoprotein that is highly expressed in various cancer cell lines and is also present in most of the glandular epithelial cells including the airway. Although the presence of numerous phosphorylation sites in its cytoplasmic domain suggests its potential role as a receptor, the unavailability of a ligand for MUC1 mucin has limited our understanding of its function. In this paper, we tried to circumvent this problem by constructing a chimeric receptor containing the cytoplasmic domain of MUC1 mucin, which can be phosphorylated on activation. To this end, we constructed a chimeric plasmid vector (pCD8/MUC1) by replacing the extracellular and transmembrane domains of human MUC1 mucin with those of human CD8. Transient transfection of the vector into COS-7 cells resulted in expression of the chimeric receptor on the surface of the COS-7 cells as judged by immunologic assays with various antibodies as well as by fluorescence-activated cell-sorting analysis. Treatment of the transfected COS-7 cells with an anti-CD8 antibody resulted in a significant increase in phosphorylation of tyrosine moieties of the chimeric receptor. This chimeric receptor will serve as a powerful tool in elucidating the signaling mechanism as well as the functional role of MUC1 mucin in the airway.

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