scholarly journals Complete sequences of epidermin and nukacin encoding plasmids from oral-derived Staphylococcus epidermidis and their antibacterial activity

2021 ◽  
Author(s):  
Kenta Nakazono ◽  
Mi Nguyen-Tra Le ◽  
Miki Kawada-Matsuo ◽  
Noy Kimheang ◽  
Junzo Hisatsune ◽  
...  
Keyword(s):  
Antibacterial Activity ◽  
Amino Acid ◽  
Staphylococcus Epidermidis ◽  
Activity Patterns ◽  
Bacterial Flora ◽  
Complete Sequence ◽  
Oral Bacteria ◽  
Amino Acid Sequences ◽  
Commensal Bacterium ◽  
Complete Sequences

AbstractStaphylococcus epidermidis is a commensal bacterium in humans. To persist in the bacterial flora of the host, some bacteria produce antibacterial factors such as the antimicrobial peptides known as bacteriocins. In this study, we tried to isolate bacteriocin-producing S. epidermidis strains. Among 150 S. epidermidis isolates from the oral cavities of 287 volunteers, we detected two bacteriocin-producing strains, KSE56 and KSE650. Complete genome sequences of the two strains confirmed that they carried the epidermin-harbouring plasmid pEpi56 and the nukacin IVK45-like- harbouring plasmid pNuk650. The amino acid sequence of epidermin from KSE56 was identical to the previously reported sequence, but the epidermin synthesis-related genes were partially different. The prepeptide amino acid sequences of nukacin KSE650 and nukacin IVK45 showed one mismatch, but both mature peptides were entirely similar. pNuk650 was larger and had an additional seven ORFs compared to pIVK45. We then investigated the antibacterial activity of the two strains against several skin and oral bacteria and found their different activity patterns. In conclusion, we report the complete sequences of 2 plasmids coding for bacteriocins from S. epidermidis, which were partially different from those previously reported. Furthermore, this is the first report to show the complete sequence of an epidermin-carrying plasmid, pEpi56.

scholarly journals Amino acid sequences of α-helical segments from S-carboxymethylkerateine-A. Complete sequence of a type-II segment

1978 ◽  
Vol 173 (2) ◽  
pp. 365-371 ◽  
Author(s):  
W G Crewther ◽  
A S Inglis ◽  
N M McKern
Keyword(s):  
Amino Acid ◽  
Coiled Coil ◽  
Complete Sequence ◽  
Amino Acid Sequences ◽  
Helical Axis ◽  
Type I ◽  
Type Ii ◽  
Coil Structure ◽  
Aqueous Urea ◽  
Alpha Keratin

1. The helical fragments obtained by partial chymotryptic digestion of S-carboxymethylkeratine-A, the low-sulphur fraction from wool, were fractionated into type-I and type-II helical segments in aqueous urea under conditions limiting carbamoylation. 2. The amino acid sequence of a 109-residue type-II segment was completed by using the sequenator. 3. When the data were incorporated into a helical model of 3.6 residues per turn the hydrophobic residues generated a band aligned at a slight angle to the helical axis. This result is in accord with the postulated coiled-coil structure of the crystalline regions of alpha-keratin.

scholarly journals The primary structure of component 8c-1, a subunit protein of intermediate filaments in wool keratin. Relationships with proteins from other intermediate filaments

1986 ◽  
Vol 236 (3) ◽  
pp. 695-703 ◽  
Author(s):  
L M Dowling ◽  
W G Crewther ◽  
A S Inglis
Keyword(s):  
Amino Acid ◽  
Intermediate Filaments ◽  
Coiled Coil ◽  
Amino Acid Sequences ◽  
British Library ◽  
Type I ◽  
Intermediate Filament Proteins ◽  
Complete Sequences ◽  
Acetyl Group ◽  
Keratin Filament

Component 8c-1, one of four highly homologous component-8 subunit proteins present in the microfibrils of wool, was isolated as its S-carboxymethyl derivative and its amino acid sequence was determined. Large peptides were isolated after cleaving the protein chemically or enzymically and the sequence of each was determined with an automatic Sequenator. The peptides were ordered by sequence overlaps and, in some instances, by homology with known sequences from other component-8 subunits. The C-terminal residues were identified by three procedures. Full details of the various procedures used have been deposited as Supplementary Publication SUP 50133 (4 pp.) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1986) 233, 5. The result showed that the protein comprises 412 residues and has an Mr, including the N-terminal acetyl group, of 48,300. The sequence of residues 98-200 of component 8c-1 was found to correspond to the partial or complete sequences of four homologous type I helical segments previously isolated from helical fragments recovered from chymotryptic digests of microfibrillar proteins of wool [Crewther & Dowling (1971) Appl. Polym. Symp. 18, 1-20; Crewther, Gough, Inglis & McKern (1978) Text. Res. J. 48, 160-162; Gough, Inglis & Crewther (1978) Biochem. J. 173, 385]. Considered in relation to amino acid sequences of other intermediate-filament proteins, the sequence is in accord with the view that keratin filament proteins are of two types [Hanukoglu & Fuchs (1983) Cell (Cambridge, Mass.) 33, 915-924]. Filament proteins from non-keratinous tissues, such as desmin, vimentin, neurofilament proteins and the glial fibrillary acidic protein, which form monocomponent filaments, constitute a third type. It is suggested that as a whole the proteins from intermediate filaments be classed as filamentins, the three types at present identified forming subgroups of this class. The significant homologies between types I, II and III occur almost exclusively in segments of the chain that have been identified as having a coiled-coil structure together with the relatively short sections connecting these segments. The non-coiled-coil segments at the C- and N-termini show no significant homology between types, nor is homology in these segments apparent in all members of one type. Component 8c-1 does not show homology in its terminal segments with the known sequence of any other filamentin.(ABSTRACT TRUNCATED AT 400 WORDS)

Modulation of anti-endotoxin property of Temporin L by minor amino acid substitution in identified phenylalanine zipper sequence

2016 ◽  
Vol 473 (21) ◽  
pp. 4045-4062 ◽  
Author(s):  
Saurabh Srivastava ◽  
Amit Kumar ◽  
Amit Kumar Tripathi ◽  
Anshika Tandon ◽  
Jimut Kanti Ghosh
Keyword(s):  
Antibacterial Activity ◽  
Amino Acid ◽  
Antimicrobial Agents ◽  
Antimicrobial Property ◽  
Antimicrobial Activities ◽  
Repeat Sequence ◽  
Amino Acid Sequences ◽  
Heptad Repeat ◽  
Plausible Mechanism ◽  
Factor Α

A 13-residue frog antimicrobial peptide Temporin L (TempL) possesses versatile antimicrobial activities and is considered a lead molecule for the development of new antimicrobial agents. To find out the amino acid sequences that influence the anti-microbial property of TempL, a phenylalanine zipper-like sequence was identified in it which was not reported earlier. Several alanine-substituted analogs and a scrambled peptide having the same composition of TempL were designed for evaluating the role of this motif. To investigate whether leucine residues instead of phenylalanine residues at ‘a’ and/or ‘d’ position(s) of the heptad repeat sequence could alter its antimicrobial property, several TempL analogs were synthesized after replacing these phenylalanine residues with leucine residues. Replacing phenylalanine residues with alanine residues in the phenylalanine zipper sequence significantly compromised the anti-endotoxin property of TempL. This is evident from the higher production of tumor necrosis factor-α and interleukin-6 in lipopolysaccharide (LPS)-stimulated rat bone-marrow-derived macrophage cells in the presence of its alanine-substituted analogs than TempL itself. However, replacement of these phenylalanine residues with leucine residues significantly augmented anti-endotoxin property of TempL. A single alanine-substituted TempL analog (F8A-TempL) showed significantly reduced cytotoxicity but retained the antibacterial activity of TempL, while the two single leucine-substituted analogs (F5L-TempL and F8L-TempL), although exhibiting lower cytotoxicity, were able to retain the antibacterial activity of the parent peptide. The results demonstrate how minor amino acid substitutions in the identified phenylalanine zipper sequence in TempL could yield analogs with better antibacterial and/or anti-endotoxin properties with their plausible mechanism of action.

scholarly journals Antibacterial Activity and Mechanism of Action of Bovine Lactoferricin Derivatives with Symmetrical Amino Acid Sequences

2018 ◽  
Vol 19 (10) ◽  
pp. 2951 ◽  
Author(s):  
Changbao Sun ◽  
Yingying Li ◽  
Songsong Cao ◽  
Haimei Wang ◽  
Chenggang Jiang ◽  
...  
Keyword(s):  
Antibacterial Activity ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Pathogenic Bacteria ◽  
Structural Parameters ◽  
Membrane Integrity ◽  
Antibacterial Properties ◽  
Scientific Basis ◽  
Amino Acid Sequences ◽  
Potential Health

In recent years, the overuse of antibiotics has become very serious. Many pathogenic bacteria have become resistant to them, with serious potential health consequences. Thus, it is urgent that we develop new antibiotic drugs. Antimicrobial peptides (AMPs) are important endogenous antibacterial molecules that contribute to immunity. Most have spectral antibacterial properties and do not confer drug resistance. In this paper, an 11-residue peptide (LFcinB18–28) with a sequence of KCRRWQWRMKK was modified by amino acid substitution to form a symmetrical amino acid sequence. The antibacterial activities and mechanisms of action of engineered peptides including KW-WK (KWRRWQWRRWK), FP-PF (FPRRWQWRRPF), FW-WF (FWRRWQWRRWF), and KK-KK (KKRRWQWRRKK) were investigated. The four engineered peptides could more effectively inhibit bacteria than the original peptide, LFcinB18–28. This suggested that a symmetrical amino acid sequence might enhance the antibacterial activity of AMPs. However, only peptides KW-WK, FP-PF, and KK-KK were safe; FW-WF displayed hemolytic activity. The engineered peptides shared cationic and amphipathic characteristics that facilitated interactions with the anionic microbial membranes, leading to disruption of membrane integrity and permeabilizing microbial membranes, resulting in cell death. Therefore, a symmetrical amino acid sequence and related structural parameters offer an alternative approach to the design of AMPs. This will provide a scientific basis for the design and synthesis of new AMPs.

scholarly journals Amino Acid Sequence Studies on Sheep Liver Fructose-bisphosphatase. II The Complete Sequence

1983 ◽  
Vol 36 (3) ◽  
pp. 235 ◽  
Author(s):  
WK Fisher ◽  
EOP Thompson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Complete Sequence ◽  
Amino Acid Sequences ◽  
Fructose Bisphosphatase ◽  
Proteolytic Digestion ◽  
Sheep Liver ◽  
Methionine Residues

The cyanogen bromide fragments of S-carboxymethylated fructose-bisphosphatase were purified. The amino acid sequences of the small fragments were determined by the dansyl-Edman method. The large fragments were subjected to proteolytic digestion to give smaller peptides more amenable for purification and sequencing by similar methods. Enzyme digests of the S-carboxymethylated enzyme gave overlap peptides containing the methionine residues.

scholarly journals Comparison of the amino acid sequences of the variable domains of two homogeneous rabbit antibodies to type III pneumococcal polysaccharide

1975 ◽  
Vol 147 (2) ◽  
pp. 235-247 ◽  
Author(s):  
J C Jaton
Keyword(s):  
Amino Acid ◽  
Complete Sequence ◽  
Amino Acid Sequences ◽  
Light Chains ◽  
Amino Acid Residues ◽  
Rabbit Antibody ◽  
Variable Regions ◽  
Type Iii ◽  
Variable Domains ◽  
V Region

The amino acid sequences of the V (variable) regions of the H (heavy) and L (light) chains derived from rabbit antibody K-25, specific for type III pneumococci, were determined; this is the second homogeneous rabbit antibody besides antibody BS-5 whose complete sequence of the V domain has been established (Jaton, 1974d). The V regions of L chains BS-5 and K-25 (both of allotype b4) differ from each other by 19 amino acid residues; 11 of these 19 substitutions are located within the three hypervariable sections of the V region. On the basis of seven amino acid differences within the N-terminal 28 positions, it is suggested that L chain K-25 belongs to a different subgroup of rabbit K chains and L chain BS-5. H chain K-25 (allotype a2) differs from another H chain of the same allotype by one amino acid substitution within the N-terminal 70 positions in addition to interchanges occurring in the first two hypervariable sections. H chain K-25 was compared with H chain BS-5 (allotype a1) and with the known V-region rabbit sequences. Allotype-related differences between a1, a2 and a3 chains appear to occur within the N-terminal 16 positions and possibly in scattered positions throughout the V-region. In the hypervariable positions, variability between the two antibodies is remarkably more pronounced within the third hypervariable section of both H and L chains than within the first two.

scholarly journals ANTIBACTERIAL ACTIVITY ETHYL ACETATE EXTRACTS OF EARTHWORMS (Lumbricus rubellus, Eisenia foetida, Nereis sp) TOWARD Staphylococcus aureus, Enterococcus faecalis, Salmonella thyposa INVITRO

el–Hayah ◽  
2019 ◽  
Vol 7 (2) ◽  
pp. 62-73 ◽  
Author(s):  
Hartati Kartikaningsih ◽  
Sarastria Maharani ◽  
Fitarina Sartika
Keyword(s):  
Amino Acids ◽  
Staphylococcus Aureus ◽  
Antibacterial Activity ◽  
Amino Acid ◽  
Ethyl Acetate ◽  
Protein Content ◽  
Enterococcus Faecalis ◽  
Amino Acid Sequences ◽  
Lumbricus Rubellus ◽  
Eisenia Foetida

Earthworms had a mechanism of antibacterial. The research aimed to observe Lumbricus rubellus, Eisenia foetida, Nereis sp. antibacterial activity against Salmonella thyposa, Staphylococcus aureus, Enterococcus faecalis in vitro compared to ampicillin antibiotics. All the worms extracted using ethyl acetate extraction and tested their MIC. The compound of amino acids of the worms was analyzed by HPLC and nanodrop.  Lumbricus rubellus was the best anti-bacteria activity followed by Eisenia foetida and Nereis sp., but these activities less than ampicillin antibiotic. Observations with SEM showed these worms extract caused cell leakage in all of these bacteria. Protein content with Nanodrop testing revealed the highest protein content was Lumbricus rubellus (21.75 ppm) followed by Eisenia foetida (21.32 ppm) and Nereis sp. (20.98 ppm), as well as for amino acids levels, there were Lumbricus rubellus (24.66%), Eisenia foetida (22.78%), Nereis sp. (18.37%). From the 15 amino acids detected, all of the worms had the same sequence of fourth the highest amino acids (Glutamate, Aspartate, Leucine, Arginine) and fourth the lowest amino acid levels (Methionine, Hystidin, Tyrosin, Glisan). It had not been tested amino acid sequences of antibacterial compounds of these worms (Lumbricin 1: Phe-Ser-Lys-Tyr-Glu-Arg in Lumbricus rubellus worms, Fetidin 1: Ala-Met-Val-Ser-Ser and Fetidin 2: Ala-Met- Val-Gly-Thr in the Eisenia foetida worm, Hemerythrin: His-Glu-Asp in Nereis sp).

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