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PubMed2007

Growth performance and ileal and total tract amino acid digestibility in broiler chickens fed diets containing bacterial protein produced on natural gas.

A total of 180 broiler chickens were fed 1 of 3 diets from day-old to slaughter at 35 d: a control diet with 35% soybean meal (SOY) or diets in which either 6% basic bacterial protein meal (BBP) or 6% autolysed bacterial protein meal (AUT) partially replaced soybean meal protein. Ileal and total tract apparent amino acid digestibility were examined in 5 chickens per diet using TiO(2) as an inert marker. Chickens fed the diets with bacterial protein had higher weight gain and feed consumption than control chicks during the first 3 wk, but there were no differences in growth or feed intake during the last 2 wk or during the total experimental period. The birds fed the BBP diet showed more efficient feed conversion compared with chickens fed the SOY and AUT diets. Litter quality at 5 wk was poorer in pens where the chickens were fed the AUT diet compared with the other 2 treatments. There were no differences among diets in the dressing percentage. Ileal amino acid digestibility at 5 wk of age revealed only minor differences between diets. There was a tendency toward lower ileal digestibility (0.12 > P > 0.07) of Arg, Lys, Met, and Phe in the AUT diet compared with the SOY diet, whereas there were no differences between the SOY and BBP diets. Total tract amino acid digestibilities at 5 wk were similar or slightly lower than the ileal digestibilities within diets. Total tract amino acid digestibility at 2 wk was similar to the total tract amino acid digestibility at 5 wk. The diets containing bacterial protein showed lower total tract digestibility of most amino acids compared with the SOY diet. It was concluded that 6% of either basic or autolysed bacterial protein can replace soybean meal in diets for broiler chickens without impairing growth performance, and the basic bacterial protein seemed to be a slightly better substitute than the autolysed bacterial protein.

Amino Acids↗
PubMed1990

Protein H--a novel IgG binding bacterial protein.

Forty-eight group A streptococcal strains of different M types were screened for binding of human radiolabeled IgG. Three of the strains bound more than 80% of the added radioactivity and one of them, an M protein type 1 strain designated AP1, was selected for further analysis. Attempts were made to solubilize the IgG binding bacterial molecule, and small amounts of an IgG binding protein with a mol. wt of 40 kDa could be solubilized with mutanolysin, a muramolytic agent. The gene encoding this streptococcal protein was cloned and expressed in E. coli, and the E. coli-produced protein was purified in a single step by affinity chromatography on IgG-Sepharose. When tested with IgGs from different species, the molecule was found to bind human IgG almost exclusively. The N-terminal amino acid sequence was determined and showed no homology with previously isolated Ig binding proteins, and the name protein H (as in human IgG) is suggested for this novel Ig binding bacterial protein. Protein H showed preferential affinity for heavy chains and Fc fragments of human IgG, and did not bind Ig light chains. The affinity constant, determined by Scatchard plots, between protein H and human polyclonal IgG was 1.6 x 10(9). No binding was observed between protein H and IgM, IgA, IgD, or IgE. Finally, when tested against several additional proteins and human plasma, protein H only showed weak binding to alpha 2-macroglobulin, a proteinase inhibitor.

Amino Acid Sequence↗
PubMed2001

Sec, drugs and rock'n'roll: antibiotic targeting of bacterial protein translocation.

A large number of bacterial proteins are active in extracytoplasmic locations. Targeting and membrane translocation of the vast majority of these secretory and membrane polypeptides is mediated by the Sec pathway. Protein secretion requires the co-ordinated and sequential action of targeting factors on the cis-side of the membrane, a complex membrane-embedded protein translocase and maturation enzymes on the trans-side. Recently, significant advances in the molecular genetics and biochemistry of the Sec pathway have revealed that several of the Sec pathway components are essential for bacterial viability and/or pathogenicity. Moreover, several biochemical assays and structural insights have become available. Importantly, some of the Sec components are unique to bacteria. These developments raise the possibility that the bacterial protein translocase and other Sec pathway components could become formidable targets for antibacterial drug discovery.

Journal Article↗
PubMed1992

Convergent evolution among immunoglobulin G-binding bacterial proteins.

Protein G, a bacterial cell-wall protein with high affinity for the constant region of IgG (IgGFc) antibodies, contains homologous repeats responsible for the interaction with IgGFc. A synthetic peptide corresponding to an 11-amino acid-long sequence in the COOH-terminal region of the repeats was found to bind to IgGFc and block the interaction with protein G. Moreover, two other IgGFc-binding bacterial proteins (proteins A and H), which do not contain any sequences homologous to the peptide, were also inhibited in their interactions with IgGFc by the peptide. Finally, a decapeptide based on a sequence in IgGFc blocked the binding of all three proteins to IgGFc. This unusually clear example of convergent evolution emphasizes the complexity of protein-protein interactions and suggests that bacterial surface-protein interaction with host protein adds selective advantages to the microorganism.

Amino Acid Sequence↗
PubMed2006

How initiation factors maximize the accuracy of tRNA selection in initiation of bacterial protein synthesis.

During initiation of bacterial protein synthesis, messenger RNA and fMet-tRNAfMet bind to the 30S ribosomal subunit together with initiation factors IF1, IF2, and IF3. Docking of the 30S preinitiation complex to the 50S ribosomal subunit results in a peptidyl-transfer competent 70S ribosome. Initiation with an elongator tRNA may lead to frameshift and an aberrant N-terminal sequence in the nascent protein. We show how the occurrence of initiation errors is minimized by (1) recognition of the formyl group by the synergistic action of IF2 and IF1, (2) uniform destabilization of the binding of all tRNAs to the 30S subunit by IF3, and (3) an optimal distance between the Shine-Dalgarno sequence and the initiator codon. We suggest why IF1 is essential for E. coli, discuss the role of the G-C base pairs in the anticodon stem of some tRNAs, and clarify gene expression changes with varying IF3 concentration in the living cell.

Bacterial Proteins↗
PubMed1994

Hormone-sensitive lipase is closely related to several bacterial proteins, and distantly related to acetylcholinesterase and lipoprotein lipase: identification of a superfamily of esterases and lipases.

We have sequenced a gene from Bacillus acidocaldarius which encodes an open reading frame (ORF3) of 310 amino acids. The ORF3 was found to be related to the mammalian hormone-sensitive lipase (HSL). Searching the protein data base revealed five other bacterial proteins related to the HSL. Upon further sequence comparisons this HSL-group was found to be related to the family of carboxylesterases, and to a family of lipases (lipoprotein, hepatic and pancreatic lipases). The evolutionary relationship of these serine-dependent hydrolytic enzymes has not been studied previously, and it has not been known that these proteins belong to the same superfamily. Finally, the alignment of the HSL with the bacterial proteins allowed us to infer the location of the hormone-sensitive regulatory domain of the HSL-protein.

Acetylcholinesterase↗
PubMed2006

Novel tetrapeptide inhibitors of bacterial protein synthesis produced by a Streptomyces sp.

In the course of a microbial product screening aimed at the discovery of novel antibiotics acting on bacterial protein synthesis, a complex of three structurally related tetrapeptides, namely, GE81112 factors A, B, and B1, was isolated from a Streptomyces sp. The screening was based on a cell-free assay of bacterial protein synthesis driven by a model mRNA containing natural initiation signals. In this study we report the production, isolation, and structure determination of these novel, potent and selective inhibitors of cell-free bacterial protein synthesis, which stably bind the 30S ribosomal subunit and inhibit the formation of fMet-puromycin. They did not inhibit translation by yeast ribosomes in vitro. Spectroscopic analyses revealed that they are tetrapeptides constituted by uncommon amino acids. While GE81112 factors A, B, and B1 were effective in inhibiting bacterial protein synthesis in vitro, they were less active against Gram-positive and Gram-negative bacterial cells. Cells grown in minimal medium were more susceptible to the compounds than those grown in rich medium, and this is most likely due to competition or regulation by medium components during peptide uptake. The novelty of the chemical structure and of the specific mode of action on the initiation phase of bacterial protein synthesis makes GE81112 a unique scaffold for designing new drugs.

Anti-Bacterial Agents↗
PubMed1984

Protein utilization in the young steer: digestion and nitrogen retention of 15N-labelled rumen bacterial protein.

15N-labelled mixed rumen bacteria, obtained from a steer that had received [15N]urea in its diet, were disrupted ultrasonically and freed from nucleic acids and their degradation products. Samples were subjected to a simulated abomasal digestion with pepsin. The digests were infused with a non-absorbable marker (polyethylene glycol) into the duodenum of four steers equipped with simple duodenal and re-entrant ileal cannulas and adapted to a diet of barley straw, flaked maize and urea. The outflow from the ileum was collected for 6-7 h. The mean value for the digestibility of 15N bacterial proteins in the small intestine was estimated to be 0.74. [14C]urea was administered intravenously during the infusion of the 15N-labelled protein into the duodenum. Urine and faeces were collected for the next 48 h and the proportion of urea-N produced, that was excreted in the urine, estimated from urine 14C excretion. Total urea 15N production was estimated from this value and the amount of 15N excreted in the urine. The mean proportion of 15N absorbed that was deposited in body protein, 0.70, was calculated by difference. The over-all efficiency of utilization of 15N in the infused rumen bacterial protein was 0.52. An approximate estimate of the mean rate of protein synthesis calculated from the data was 24 g/kg body-weight (W)0.75 per d and compared with an estimated net deposition of protein of 1.67 g/kg (W)0.75 per d. The importance of these values in factorial schemes for estimating ruminant N requirements is discussed.

Animals↗
PubMed2006

Agarose isoelectric focusing can improve resolution of membrane proteins in the two-dimensional electrophoresis of bacterial proteins.

2-D separation of bacterial membrane proteins is still difficult despite using high-resolution IPG-IEF/SDS-PAGE. We were searching for alternative methods to avoid typical problems such as precipitation, low solubility, and aggregation of membrane proteins in the 1-D separation with IPG-IEF. Blue native electrophoresis (BNE) and agarose IEF (A-IEF) were tested for their separation capacity and their capability of replacing IPG-IEF in the first dimension. SDS-PAGE was chosen for the second dimension on account of its outstanding resolution. We could confirm that only A-IEF was a useful replacement for the IPG-IEF in the first dimension resulting in 2-D protein distributions with additional membrane protein spots not being found after IPG-IEF/SDS-PAGE. A second interesting result was that the agarose IEF mediates the possibility of separation of membrane proteins in a partially native state in the first dimension. This native A-IEF resulted in drastically changed spot patterns with an acidic shift of nearly all spots and divergent distribution of proteins compared to non-native A-IEF and IPG-IEF. We found out that native and non-native A-IEF are powerful tools to supplement IPG-IEF/SDS-PAGE.

Bacterial Proteins↗
PubMed1992

Effect of dietary amino acids on in vitro rumen bacterial protein synthesis in buffaloes.

The effect of different ratios of urea to amino acid N at a fixed concentration of soluble sugars as energy source and varying levels of soluble sugars at optimum urea cell suspension was obtained from the rumen fluid of buffalo (Bubalus bubalis) calves fed on a growth ration. Under glucose fermentation, the bacterial protein content of the incubation mixture (I. M.) was increased to 3.91, 6.31 and 5.08 times the control value (urea alone) when 25, 50 and 75% of urea-N was replaced with amino acid N, respectively. With cellobiose, the corresponding increase was 4.06, 5.29 and 5.63 times. At 50% urea-N replacement with amino acid N (a ratio for maximum protein synthesis), the bacterial content was maximum when 1 g glucose or cellobiose per 100 ml of I. M. was added. Per cent incorporation of radioactivity from amino acids into bacterial protein was maximum at 25% amino acid N level with both the soluble sugar sources. The total amino acids incorporated into bacterial protein were, however, more at 50% than at 25% amino acid N level.

Amino Acids↗
PubMed1994

Protein PAB, a mosaic albumin-binding bacterial protein representing the first contemporary example of module shuffling.

Some strains of the anaerobic human commensal and pathogen Peptostreptococcus magnus bind human serum albumin (HSA), whereas other strains of this species express protein L, an immunoglobulin light chain-binding surface protein. A novel HSA-binding protein called protein PAB was purified in one step from the culture supernatant of an HSA-binding strain of P. magnus by affinity chromatography on HSA-Sepharose. The apparent size of the molecular was 47 kDa on SDS-polyacrylamide gel electrophoresis. Amino acid sequence analysis of protein PAB demonstrated that the 4 NH2-terminal residues were identical to the corresponding sequence in protein L. In a polymerase chain reaction, oligonucleotides based on extragenic 5'- and 3'-end sequences of the protein L gene generated a product of the expected size: 1.3 kilobase pairs. A recombinant protein with retained albumin binding capacity was expressed in Escherichia coli, and the nucleotide sequence of the protein PAB gene was determined. The structural gene is 1161 nucleotides long, corresponding to a preprotein of 387 amino acids and a molecular mass of 43,043 Da. Unlike most other Gram-positive bacterial surface proteins described, protein PAB contains no internal homologies. However, substantial homologies were found to both proteins L and G (the IgG- and HSA-binding surface protein of group C and G streptococci). The derived amino acid sequence of the 135-base pair-long region homologous to protein G corresponds to the HSA-binding domain of that protein, and in protein PAB, this region is inserted between sequences showing extensive homology to COOH-terminal regions of peptostreptococcal protein L. This mosaic organization of protein PAB demonstrates that the molecule is a product of intergenic interspecies recombination of a functional domain into a common framework for peptostreptococcal surface proteins. Such an interspecies exchange of a functional protein module has previously not been described in prokaryotic cells.

Amino Acid Sequence↗
PubMed1987

Factors affecting the rate of breakdown of bacterial protein in rumen fluid.

1. The cellular proteins of Butyrivibrio fibrisolvens, Lactobacillus casei, Megasphaera elsdenii, Selenomonas ruminantium and Streptococcus bovis were labelled by growth in the presence of L-[14C]leucine, and the breakdown of labelled protein was measured in incubations of these bacteria with rumen fluid to which unlabelled 5 mM-L-leucine was added. The rate of protein breakdown was estimated from the rate of release of radioactivity into acid-soluble material. 2. Protein breakdown occurred at different rates in different species. The mean rates for B. fibrisolvens, L. casei, M. elsdenii, Sel. ruminantium and Str. bovis were 28.6, 18.1, 17.7, 10.5 and 5.3%/h respectively in samples of strained rumen fluid (SRF) with different protozoal populations. Rates of 3%/h or less were found in SRF from ciliate-free sheep or in faunated SRF from which protozoa had been removed by centrifugation. Further removal of mixed rumen bacteria had little effect. Suspensions of washed protozoa degraded bacterial protein at rates which were of the same order as those found in SRF. 3. The rate of breakdown of bacterial protein in different samples of SRF tended to increase as the numbers of small entodiniomorphid protozoa increased. The numbers of larger entodiniomorphs and holotrichs had no obvious influence on this rate. 4. Autoclaved and u.v.-treated bacteria were generally no different from live bacteria in their susceptibility to breakdown in SRF from faunated sheep, indicating that endogenous protein turnover was not a significant cause of bacterial protein catabolism. 5. The rate of bacterial protein breakdown was unrelated to the proteolytic activity of SRF. 6. It was concluded that predation by small protozoa is by far the most important cause of bacterial protein turnover in the rumen, with autolysis, other lytic factors and endogenous proteolysis being of minor importance.

Animals↗
PubMed2003

Structural determinants of SecB recognition by SecA in bacterial protein translocation.

SecB is a bacterial chaperone involved in directing pre-protein to the translocation pathway by its specific interaction with the peripheral membrane ATPase SecA. The SecB-binding site on SecA is located at its C terminus and consists of a stretch of highly conserved residues. The crystal structure of SecB in complex with the C-terminal 27 amino acids of SecA from Haemophilus influenzae shows that the SecA peptide is structured as a CCCH zinc-binding motif. One SecB tetramer is bound by two SecA peptides, and the interface involves primarily salt bridges and hydrogen bonding interactions. The structure explains the importance of the zinc-binding motif and conserved residues at the C terminus of SecA in its high-affinity binding with SecB. It also suggests a model of SecB-SecA interaction and its implication for the mechanism of pre-protein transfer in bacterial protein translocation.

Adenosine Triphosphatases↗
PubMed1994

Dentin permeability to bacterial proteins in vitro.

Passage of bacterial components through dentin is a subject of recent research with in vitro as well as with in vivo models. Diffusive transport of Porphyromonas gingivalis ATCC 33277 proteins has been demonstrated by the authors with an in vitro setup closely simulating the pulp chamber. The purpose of this investigation was to study the filtration of these proteins through dentin, measure possible concentration changes resulting from the filtering, and elaborate on the physical aspects of the binding process. The hydraulic conductance (Lp) of 10 dentin specimens was determined in three experiments using standard procedures: initially with phosphate-buffered saline, subsequently with a P. gingivalis ATCC 33277 suspension (200 micrograms/ml of protein), and finally with phosphate-buffered saline. The results showed significant, nonpermanent, alterations of the Lps of the dentin disks, and variable retention of the bacterial proteins among samples. A positive correlation between the bacterial protein retention and reduction of Lps was also demonstrated. The reduction of the Lps of the dentin samples was attributed to microstructural changes of the dentin, while the bacterial protein retention was considered to take place either on the surface of the disk or intratubularly. The intratubular interactions in the present experiment seemed to have a mechanical rather than a chemical basis.

Bacterial Proteins↗
PubMed1984

[Nitrogen metabolism in growing swine receiving a bacterial protein supplement (Alcaligenes eutrophus) instead of soybean meal].

In a balance trial with 10 pigs (mean body mass 50 kg) the influence of a bacterial protein supplement (Alcaligenes eutrophus) on N-metabolism was investigated. The bacteria were included into the diet at levels of 7 and 14% at the expense of extracted soyabean meal. Thus bacterial "pure protein" (bacterial non-nucleic acid N X X 6.25) amounted to 30 and 60% of the protein of the ration. Consuming 2 kg of feed dry matter per day the animals of the control group (I) and the experimental groups (II and III) ingested 48 g, 52 g and 55 g of total N respectively. The difference in N-intake is explained by the additional nucleic acid-N, amounting to 19,8% of total bacterial N. Daily weight gain (on average 1054 g) and feed conversion efficiency (feed ingested/weight gain; on average 1,9) were relatively improved at the highest dietary level of bacterial cell mass. Faecal N-excretion was increased significantly, whereas renal N-excretion remained unchanged. Mean apparent N-digestibility was 87,4% showing no significant difference between the experimental groups. N-balance values were noticibly increased following the intake of the bacterial protein supplement. The excretion of urinary urea-N was slightly reduced whereas 4-6 times as much allantoin-N was excreted when bacteria were fed. It is calculated that about 80% of the bacterial purines are renally excreted as allantoin and uric acid.

Alcaligenes↗
PubMed1982

Thin layer iso-electro focusing of intracellular bacterial protein in classification of some representatives of the families Enterobacteriaceae and Vibrionaceae.

Intracellular bacterial protein from some representatives of the families Enterobacteriaceae and Vibrionaceae has been investigated using thin layer iso-electric focusing in polyacrylamide gel. A marked difference between the protein patterns was observed between species within the same family. Carrying out the iso-electric focusing at pH range 3.5-9 gave a large number of protein bands. Increased resolution of the protein bands was obtained using iso-electric focusing at the pH range 4-6.5. Careful standardization of sample preparation, application and running conditions gave good reproducibility of intracellular proteins from bacterial subcultures.

Aeromonas↗
PubMed2000

The biogenesis and assembly of bacterial membrane proteins.

Bacterial proteins in the inner and outer membranes differ dramatically in their architecture. Although both types of proteins are transported across the inner membrane through a common pore, recent studies have identified distinct factors that target them to transport sites and catalyze proper folding.

Bacterial Outer Membrane Proteins↗