Functional stirred Yoghurt fortified with buffalo, bovine, mix colostrum and lactoferrin, effect of lactoferrin on pathogenic bacteria and amino acids of buffalo, bovine colostrum and lactoferrin

2021 ◽  
Vol 0 (0) ◽  
pp. 0-0
Author(s):  
Hamdy Shaaban ◽  
Alshymaa Karam-Allah ◽  
Eman Abo-Zaid ◽  
Mahmoud refae ◽  
Sherif saad ◽  
...  
Keyword(s):  
Amino Acids ◽  
Pathogenic Bacteria ◽  
Bovine Colostrum

scholarly journals The Human CXC Chemokine Granulocyte Chemotactic Protein 2 (GCP-2)/CXCL6 Possesses Membrane-Disrupting Properties and Is Antibacterial

2008 ◽  
Vol 52 (7) ◽  
pp. 2599-2607 ◽  
Author(s):  
Helena M. Linge ◽  
Mattias Collin ◽  
Pontus Nordenfelt ◽  
Matthias Mörgelin ◽  
Martin Malmsten ◽  
...  
Keyword(s):  
Amino Acids ◽  
Antibacterial Activity ◽  
Pathogenic Bacteria ◽  
Membrane Disruption ◽  
Minimal Bactericidal Concentration ◽  
Bacterial Surface ◽  
Bacterial Membranes ◽  
Chemotactic Protein ◽  
Cxc Chemokine ◽  
Α Helix

ABSTRACT Granulocyte chemotactic protein 2 (GCP-2)/CXCL6 is a CXC chemokine expressed by macrophages and epithelial and mesenchymal cells during inflammation. Through binding and activation of its receptors (CXCR1 and CXCR2), it exerts neutrophil-activating and angiogenic activities. Here we show that GCP-2/CXCL6 itself is antibacterial. Antibacterial activity against gram-positive and gram-negative pathogenic bacteria of relevance to mucosal infections was seen at submicromolar concentrations (minimal bactericidal concentration at which 50% of strains tested were killed, 0.063 ± 0.01 to 0.37 ± 0.03 μM). In killed bacteria, GCP-2/CXCL6 associated with bacterial surfaces, which showed membrane disruption and leakage. A structural prediction indicated the presence of three antiparallel NH2-terminal β-sheets and a short amphipathic COOH-terminal α-helix; the latter feature is typical of antimicrobial peptides. However, when the synthetic derivatives corresponding to the NH2-terminal (50 amino acids) and COOH-terminal (19 amino acids, corresponding to the putative α-helix) regions were compared, higher antibacterial activity was observed for the NH2-terminus-derived peptide, indicating that the holopeptide is necessary for full antibacterial activity. An artificial model of bacterial membranes confirmed these findings. The helical content of GCP-2/CXCL6 in the presence or absence of lipopolysaccharide or negatively charged membranes was studied by circular dichroism. As with many antibacterial peptides, membrane disruption by GCP-2/CXCL6 was dose-dependently reduced in the presence of NaCl, which, we here demonstrate, inhibited the binding of the peptide to the bacterial surface. Compared with CXC chemokines ENA-78/CXCL5 and NAP-2/CXCL7, GCP-2/CXCL6 showed a 90-fold-higher antibacterial activity. Taken together, GCP/CXCL6, in addition to its chemotactic and angiogenic properties, is likely to contribute to direct antibacterial activity during localized infection.

scholarly journals Synthesis, Characterization, and Antibacterial Studies of Mixed Ligand Dioxouranium Complexes with 8-Hydroxyquinoline and Some Amino Acids

2011 ◽  
Vol 2011 ◽  
pp. 1-6 ◽  
Author(s):  
Sunil S. Patil ◽  
Ganesh A. Thakur ◽  
Manzoor M. Shaikh
Keyword(s):  
Amino Acids ◽  
Magnetic Susceptibility ◽  
Metal Ion ◽  
Pathogenic Bacteria ◽  
Electronic Absorption Spectra ◽  
Thermal Studies ◽  
Electrical Conductance ◽  
Analysis Data ◽  
Mixed Ligand ◽  
Nmr Studies

Mixed ligand complexes of dioxouranium (VI) of the type [UO2(Q)(L)·2H2O] have been synthesized using 8-hydroxyquinoline (HQ) as a primary ligand and amino acids (HL) such as L-threonine, L-tryptophan, and L-isoleucine as secondary ligands. The metal complexes have been characterized by elemental analysis, electrical conductance, magnetic susceptibility measurements, and spectral and thermal studies. The electrical conductance studies of the complexes indicate their nonelectrolytic nature. Magnetic susceptibility measurements revealed diamagnetic nature of the complexes. Electronic absorption spectra of the complexes show intraligand and charge transfer transitions, respectively. Bonding of the metal ion through N- and O-donor atoms of the ligands is revealed by IR studies, and the chemical environment of the protons is confirmed by NMR studies. The thermal analysis data of the complexes indicate the presence of coordinated water molecules. The agar cup and tube dilution methods have been used to study the antibacterial activity of the complexes against the pathogenic bacteria S. aureus, C. diphtheriae, S. typhi, and E. coli.

Metabolomics methods to analyze full spectrum of amino acids in different domains of bovine colostrum and mature milk

2019 ◽  
Vol 246 (1) ◽  
pp. 213-224 ◽  
Author(s):  
Mohan Li ◽  
Weixuan Li ◽  
Fanhua Kong ◽  
Shimo Kang ◽  
Xiaona Liang ◽  
...  
Keyword(s):  
Amino Acids ◽  
Bovine Colostrum ◽  
Mature Milk ◽  
Full Spectrum

scholarly journals Comparative Genomics Revealed Genus Specific Encoding of Amino Acids by Tri-Nucleotide SSRs in Human Pathogenic Streptococcus and Staphylococus Bacteria

2022 ◽  
Author(s):  
Sahil Mahfooz ◽  
Jitendra Narayan ◽  
Ruba Mustafa Elsaid Ahmed ◽  
Amel Bakri Mohammed El Hag ◽  
Nuha Abdel Rahman Khalil Mohammed ◽  
...  
Keyword(s):  
Amino Acids ◽  
Pathogenic Bacteria ◽  
Repetitive Sequences ◽  
Phase Variation ◽  
Housekeeping Genes ◽  
Phase Variable ◽  
Human Pathogens ◽  
Adaptation Mechanism ◽  
Intergenic Sequences ◽  
Intergenic Regions

Abstract Pathogenic bacteria use phase variation of surface molecules and other characteristics as a significant adaptation mechanism. Repetitive sequences made up of numerous identical repeat units can be found in many phase variable genes. Here, we investigated the frequency and distribution of long-SSRs in 15 human pathogenic Staphylococcus, Streptococcus, and Enterococcus bacteria. Long-SSRs were found to be distributed differently in the genic and intergenic sequences. In the genic sequences, 61.3 SSRs were discovered on average, while 16.2 SSRs were found in the intergenic regions. Staphylococci exhibited the highest frequency of SSRs, followed by Enterococcus, and Streptococci had the lowest frequency of SSRs. Higher A+T content was found to be the best predictor of long-SSR in these human pathogens. Tetranucleotide repeats predominated in intergenic regions, while trinucleotide repeats predominated in genic regions. In human pathogenic Streptococcus and Staphylococcus bacteria, genus-specific encoding of amino acids by tri-nucleotide SSRs was observed. A genetic relationship between these human pathogenic bacteria was derived based on the presence of SSRs in the housekeeping genes and compared to the phylogeny generated based on the 16S ribosomal RNA gene.

Quantitative analysis of amino acids in human and bovine colostrum milk samples through iTRAQ labeling

2018 ◽  
Vol 98 (13) ◽  
pp. 5157-5163 ◽  
Author(s):  
Xiaona Liang ◽  
Hongjiao Han ◽  
Xue Zhao ◽  
Xueyan Cao ◽  
Mei Yang ◽  
...  
Keyword(s):  
Amino Acids ◽  
Quantitative Analysis ◽  
Bovine Colostrum ◽  
Itraq Labeling ◽  
Milk Samples

scholarly journals ARGININE-RICH PROTEINS OF POLYMORPHONUCLEAR LEUKOCYTE LYSOSOMES

1968 ◽  
Vol 127 (5) ◽  
pp. 927-941 ◽  
Author(s):  
H. I. Zeya ◽  
J. K. Spitznagel
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Staphylococcus Aureus ◽  
Amino Acid ◽  
Pathogenic Bacteria ◽  
Aromatic Amino Acids ◽  
Electrophoretic Mobilities ◽  
Low Concentrations ◽  
Different Cultures ◽  
Very High

The cationic antibacterial proteins of rabbit PMN lysosomes have been resolved into at least five subfractions. Each of these showed substantial selectivity in its antibacterial action against several pathogenic bacteria, including two smooth and two rough Escherichia coli strains, three Staphylococcus aureus strains, one S. albus, three proteus species and four different cultures of streptococcus. Each of the subfractions possesses a different electrophoretic mobility. Amino acid analyses of the three most cationic components revealed high contents of arginine consistent with their relative electrophoretic mobilities and very high arginine to lysine ratios. Aromatic amino acids were present in very low concentrations in these proteins and their light absorption at 2800 A was correspondingly weak. The evidence of antibacterial specificity, along with marked differences in the arginine-lysine ratios, shows that the cationic antibacterial components of rabbit PMN lysosomes are biologically and chemically heterogeneous.

scholarly journals Two Domains within the Mycoplasma hyopneumoniae Cilium Adhesin Bind Heparin

2006 ◽  
Vol 74 (1) ◽  
pp. 481-487 ◽  
Author(s):  
Cheryl Jenkins ◽  
Jody L. Wilton ◽  
F. Chris Minion ◽  
Linda Falconer ◽  
Mark J. Walker ◽  
...  
Keyword(s):  
Amino Acids ◽  
Pathogenic Bacteria ◽  
Mycoplasma Hyopneumoniae ◽  
Binding Activity ◽  
Sulfated Polysaccharides ◽  
Heparin Binding ◽  
Swine Production ◽  
C Terminus ◽  
Respiratory Cilia ◽  
Ciliated Epithelial Cells

ABSTRACT Mycoplasma hyopneumoniae is the causative agent of porcine enzootic pneumonia, a chronic and economically significant respiratory disease that affects swine production worldwide. M. hyopneumoniae adheres to and adversely affects the function of ciliated epithelial cells of the respiratory tract, and the cilium adhesin (Mhp183, P97) is intricately but not exclusively involved in this process. Although binding of pathogenic bacteria to glycosaminoglycans is a recognized step in pathogenesis, knowledge of glycosaminoglycan-binding proteins in M. hyopneumoniae is lacking. However, heparin and other sulfated polysaccharides are known to block the binding of M. hyopneumoniae to purified swine respiratory cilia. In this study, four regions within the cilium adhesin were examined for the ability to bind heparin. Cilium adhesin fragments comprising 653 amino acids of the N terminus and 301 amino acids of the C terminus (containing two repeat regions, R1 and R2) were cloned and expressed. These fragments bound heparin in a dose-dependent and saturable manner with physiologically significant binding affinities of 0.27 ± 0.02 μM and 1.89 ± 0.33 μM, respectively. Heparin binding of both fragments was strongly inhibited by the sulfated polysaccharides fucoidan and mucin but not by chondroitin sulfate B. When the C-terminal repeat regions R1 and R2 were cloned separately and expressed, heparin-binding activity was lost, suggesting that both regions are required for heparin binding. The ability of the cilium adhesin to bind heparin indicates that this molecule plays a multifunctional role in the adherence of M. hyopneumoniae to host respiratory surfaces and therefore has important implications with respect to the pathogenesis of this organism.

Utilization of carbon sources by clinical isolates ofAeromonas

2017 ◽  
Vol 63 (4) ◽  
pp. 359-364 ◽  
Author(s):  
Karoline C. Prediger ◽  
Monica Surek ◽  
Cibelle B. Dallagassa ◽  
Flávia E.A. Assis ◽  
Mario S. Piantavini ◽  
...  
Keyword(s):  
Amino Acids ◽  
Pathogenic Bacteria ◽  
Carbon Sources ◽  
Aquatic Organisms ◽  
Wound Infections ◽  
Human Intestine ◽  
Common Condition ◽  
Intestinal Mucin ◽  
Carbon Substrates

Bacteria in the genus Aeromonas are primarily aquatic organisms; however, some species can cause diseases in humans, ranging from wound infections to septicemia, of which diarrhea is the most common condition. The ability to use a variety of carbon substrates is advantageous for pathogenic bacteria. Therefore, we used Biolog GN2 microplates to analyze the ability of 103 clinical, predominantly diarrheal, isolates of Aeromonas to use various carbon sources, and we verified whether, among the substrates metabolized by these strains, there were some endogenous to the human intestine. The results indicate that Aeromonas present great diversity in the utilization of carbon sources, and that they preferentially use carbohydrates and amino acids as carbon sources. Among the carbon sources metabolized by Aeromonas in vitro, some were found to be components of intestinal mucin, including aspartic acid, glutamic acid, l-serine, galactose, N-acetyl-glucosamine, and glucose, which were used by all strains tested. Additionally, mannose, d-serine, proline, threonine, and N-acetyl-galactosamine were used by several strains. The potential to metabolize substrates endogenous to the intestine may contribute to Aeromonas’ capacity to grow in and colonize the intestine. We speculate that this may help explain the ability of Aeromonas to cause diarrhea.

scholarly journals Antibacterial Properties of Melanoidins Produced from Various Combinations of Maillard Reaction against Pathogenic Bacteria

2021 ◽  
Author(s):  
Satoshi Kukuminato ◽  
Kento Koyama ◽  
Shigenobu Koseki
Keyword(s):  
Amino Acids ◽  
Antimicrobial Activity ◽  
Maillard Reaction ◽  
Pathogenic Bacteria ◽  
Reducing Sugars ◽  
Antibacterial Properties ◽  
Antimicrobial Effect

Although the antimicrobial effect of melanoidins has been reported in some foods, there have been few comprehensive investigations on the antimicrobial activity of combinations of reaction substrates of the Maillard reaction. The present study comprehensively investigated the potential of various combinations of reducing sugars and amino acids. Because the melanoidins examined in this study were produced simply by heating in an autoclave at 121°C for 60 min, the of the targeted melanoidins can be easily produced.

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