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PubMed1992

Eight bacterial proteins, including UDP-N-acetylglucosamine acyltransferase (LpxA) and three other transferases of Escherichia coli, consist of a six-residue periodicity theme.

Only a few prokaryotic or eukaryotic enzymes are known to consist of a tandem-repeat structure. This report describes a common hexapeptide-repeat theme in four Escherichia coli transferases and in four less-characterized bacterial proteins. The proteins are the Ssc protein of Salmonella typhimurium (25), UDP-N-acetylglucosamine acyltransferase of E. coli (24), the hypothetical proteins Tms of Bacillus subtilis (23) and Yglm of E. coli (22), succinyldiaminopimelate aminotransferase of E. coli (14), serine acetyltransferase of E. coli (13), NodL of Rhizobium leguminasorum (13), and thiogalactoside acetyltransferase of E. coli (8) (number of repeats indicated in parentheses). In UDP-N-acetylglucosamine acyltransferase, the repeats constitute 55% of the total protein. Each hexapeptide repeat of the eight proteins starts with Ile, Leu, or Val. Position b is occupied by Gly, position d by Gly, Asn, or Asp, and position e by Val or Ala in 52%, 54%, and 56% of the hexapeptide repeats, respectively.

Acetyltransferases↗
PubMed2003

Ruminal fermentation and bacterial protein synthesis of whole cottonseed coated with combinations of gelatinized corn starch and urea.

Four ruminally and duodenally cannulated Jersey cows were used in a 4 x 5 incomplete Latin square study to determine the effects of including urea in the gelatinized corn starch coating applied to whole cottonseed (WCS) on ruminal fermentation, fiber digestion, and bacterial protein synthesis. Treatments included uncoated WCS (control) and four coated WCS treatments. The coatings provided two concentrations each of gelatinized corn starch (2.5 [2S] or 5% [5S]) and feed grade urea (0.25 [2U] or 0.5% [5U]). Treated WCS comprised 15% of the ration dry matter that was fed as a total mixed ration once daily. Ruminal pH and molar proportions of isobutyrate was higher and NH3-N concentrations lower for control compared with coated WCS. Molar proportions of propionate tended to be higher and valerate was lower with 2S compared with 5S. Molar proportions of acetate tended to be lower, whereas butyrate was higher for 5U than 2U. Nutrient intake was lower for WCS coated with 5S5U compared with 2S5U. Ruminal NDF digestibility of NDF tended to be higher with 5U compared with 2U, but no differences were observed in ruminal or total tract apparent digestibility of nutrients. No differences were observed in the flow of total N or bacterial N to the duodenum, but the flow of nonbacterial N tended to be higher for WCS coated with 5U. Coating WCS appears to slightly alter ruminal metabolism while providing similar amounts of N flowing to the duodenum without altering fiber digestion.

Animal Feed↗
PubMed1996

Persistence of serum and salivary antibody responses after oral immunization with a bacterial protein antigen genetically linked to the A2/B subunits of cholera toxin.

Primary oral immunization of mice with a bacterial protein antigen genetically coupled to the A2 and B subunits of cholera toxin induced specific secretory immunoglobulin A and serum immunoglobulin G antibodies that persisted at substantial levels for at least 11 months. A subsequent single booster immunization did not further enhance the antibody responses. Long-term antibody persistence may be especially important in infections caused by common pathogens for which continuous immunity would be advantageous.

Adhesins, Bacterial↗
PubMed1996

Salivary, nasal, genital, and systemic antibody responses in monkeys immunized intranasally with a bacterial protein antigen and the Cholera toxin B subunit.

Previous attempts to induce mucosal antibodies in rhesus monkeys by enteric immunization have resulted in only modest and short-lived responses, dominated by immunoglobulin M (IgM) antibodies in the plasma. In this study, two groups of rhesus monkeys were immunized intranasally three times at 2-week intervals with a bacterial protein antigen (AgI/II) either chemically coupled to or mixed with the B subunit of cholera toxin (CT), a known potent mucosal immunogen and carrier for other immunogens. Cells secreting antibodies, predominantly of the IgA isotype, to AgI/II and to CT were detected in the peripheral blood 1 week after each immunization, indicating the dissemination of IgA-secreting precursor cells through the mucosal immune system. IgG and, to a lesser extent, IgA antibodies to both proteins were induced in the plasma commencing after the second immunization. Plasma IgE concentrations and IgE antibody levels were not consistently raised during the immunization period. IgA antibodies were found in nasal and vaginal washes. Nasal IgG but not IgA antibodies showed a significant positive correlation with plasma IgG antibody levels, suggesting that they were largely derived by transudation from the circulation. Analysis of the molecular form of vaginal IgA indicated that both secretory and monomeric forms of IgA were present in various proportions. Furthermore, neither IgG nor IgA antibodies in vaginal washes were correlated with plasma antibody responses, suggesting the contribution of locally synthesized antibodies of both isotypes. Comparison of the responses between the two groups of animals showed only sporadic significant differences, indicating that intranasal immunization with AgI/II either coupled to or mixed with the B subunit of CT was equally effective at inducing generalized IgA antibody responses in the mucosal immune system and predominantly IgG antibodies in the plasma.

Administration, Intranasal↗
PubMed1995

Secretion of a bacterial protein by mammalian cells.

The MalE protein is a periplasmic maltooligosaccharide binding protein from Escherichia coli. This protein is widely used as a model for protein export in bacteria and as a vector for the export and one-step affinity purification of foreign polypeptides. Expression of MalE was studied in various animal cell lines. The protein was exported into the culture medium, following the classical pathway of eukaryotic protein secretion. This was shown by a combination of approaches including the use of inhibitors of the Golgi complex and immunocytological methods. The signal sequence of MalE is required for secretion and a specific signal can be added to MalE that targets it to the endoplasmic reticulum. This work opens the way to the study of the secretion of a bacterial protein and to its use as a vector for protein secretion and purification from mammalian cells.

ATP-Binding Cassette Transporters↗
PubMed2000

Crystal structure of the bacterial protein export chaperone secB.

SecB is a bacterial molecular chaperone involved in mediating translocation of newly synthesized polypeptides across the cytoplasmic membrane of bacteria. The crystal structure of SecB from Haemophilus influenzae shows that the molecule is a tetramer organized as a dimer of dimers. Two long channels run along the side of the molecule. These are bounded by flexible loops and lined with conserved hydrophobic amino acids, which define a suitable environment for binding non-native polypeptides. The structure also reveals an acidic region on the top surface of the molecule, several residues of which have been implicated in binding to SecA, its downstream target.

Adenosine Triphosphatases↗
PubMed1987

Bacterial membrane proteins.

Bacterial membranes have diverse functions, depending on whether they are specialized membranes or cytoplasmic membranes possessing transport, mitochondrial activities and biosynthetic functions for assembly of membranes, walls and capsules. In contrast to plasma membranes which serve as major biochemical organelles of both Gram-positive and Gram-negative bacteria, the outer membranes of the latter group confer barrier functions on the cells, providing a variety of selective channels. Although prokaryotic cells lack the array of membranous organelles characteristic of eukaryotic cells, bacteria with specific physiological and genetic capabilities form specialized membrane systems such as the bacteriorhodopsin purple membrane, chromatophore membranes of phototrophs, and forespore membranes essential to bacterial endospore formation. Unravelling the structure, function and proteins of these membranes presents a formidable biochemical, immunochemical and structural challenge.

Bacterial Outer Membrane Proteins↗
PubMed1976

Inhibition by thiopeptin of bacterial protein synthesis.

Thiopeptin, a sulfur-containing antibiotic, was found to inhibit protein synthesis in a bacterial ribosomal system. The pretreatment of ribosomal subunits with the antibiotic revealed that thiopeptin may act on the 50 S ribosomal subunit. The elongation of peptide chain on the ribosome is more profoundly blocked by the antibiotic than the initiation of protein synthesis. It was demonstrated that thiopeptin inhibits elongation factor (EF)-Tu-dependent GTP hydrolysis and binding of aminoacyl-tRNA to the ribosome. The peptidyl transferase-catalyzed puromycin reaction is not significantly affected by the antibiotic. Thiopeptin inhibits EF-G-associated GTPase reaction, and translocation of peptidyl-tRNA and mRNA from the acceptor site to the donor site. Protein synthesis in ribosomal systems, obtained from rat liver and rabbit reticulocytes are insensitive to the antibiotic.

Anti-Bacterial Agents↗
PubMed2002

Nonsecreted bacterial proteins induce recall CD8 T cell responses but do not serve as protective antigens.

Secreted or nonsecreted Ag expressed by recombinant Listeria monocytogenes can prime CD8 T cells. However, Ag-specific memory CD8 T cells confer protection against bacteria secreting Ag, but not against bacteria expressing the nonsecreted form of the same Ag. This dichotomy may be explained by a long-standing hypothesis that nonsecreted Ags are less effective than secreted Ags at inducing a protective immune response at the onset of infection. We tested this hypothesis by examining whether these two different forms of Ag induce different primary and secondary CD8 T cell responses. The primary responses to secreted and nonsecreted Ags expanded and contracted almost synchronously, although the responses to nonsecreted Ags were of lower magnitude. These results demonstrate that the kinetics of the CD8 T cell response are similar regardless of whether Ag is accessible to the endogenous MHC class I pathway or can only be presented through cross-presentation. No differences were detected in the CD8 T cell recall response to L. monocytogenes expressing secreted or nonsecreted Ags. Nonsecreted Ags are as effective as secreted Ags at the induction of a rapid recall response by memory CD8 T cells. Thus, the inability of nonsecreted bacterial proteins to serve as protective Ags cannot be attributed to a defective CD8 T cell response.

Animals↗
PubMed2006

Gene fusion/fission is a major contributor to evolution of multi-domain bacterial proteins.

Most proteins comprise one or several domains. New domain architectures can be created by combining previously existing domains. The elementary events that create new domain architectures may be categorized into three classes, namely domain(s) insertion or deletion (indel), exchange and repetition. Using 'DomainTeam', a tool dedicated to the search for microsyntenies of domains, we quantified the relative contribution of these events. This tool allowed us to collect homologous bacterial genes encoding proteins that have obviously evolved by modular assembly of domains. We show that indels are the most frequent elementary events and that they occur in most cases at either the N- or C-terminus of the proteins. As revealed by the genomic neighbourhood/context of the corresponding genes, we show that a substantial number of these terminal indels are the consequence of gene fusions/fissions. We provide evidence showing that the contribution of gene fusion/fission to the evolution of multi-domain bacterial proteins is lower-bounded by 27% and upper-bounded by 64%. We conclude that gene fusion/fission is a major contributor to the evolution of multi-domain bacterial proteins.

Bacterial Proteins↗
PubMed1990

Monoclonal antibodies against an HLA-B27-derived peptide react with an epitope present on bacterial proteins.

The role of molecular mimicry in the spondyloarthropathies was investigated with respect to the epitopes involved. mAb were produced against a synthetic peptide whose sequence was derived from a polymorphic region of the HLA-B27 molecule (amino acids 63-83). Two antibodies (J7F2 and H2B6) were selected for study on the basis of their ability to react with bacterial envelope proteins (ELISA) and B27-positive cells (immunofluorescence). J7F2 reacted preferentially with B27-positive cells and neither antibody reacted with MHC class I negative cells. Based on SDS-PAGE blot analysis of bacterial envelope proteins, the pattern of reactivity for both antibodies (against 36- and 19-kDa proteins) was the same as that for a third monoclonal produced against bacterial envelope and reactive with B27-positive cells. This apparent epitope similarity was investigated by using synthetic peptides to inhibit binding of the monoclonals. The B27 synthetic peptide and a smaller peptide derived from it were efficient inhibitors of antipeptide and antibacterial antibody binding to bacterial Ag and B27-positive cells. These studies provide insight into the molecular basis of cross-reactivity between bacterial proteins and MHC class I molecules.

Amino Acid Sequence↗
PubMed1995

Interaction of the bacterial protein toxin alpha-haemolysin with model membranes: protein binding does not always lead to lytic activity.

alpha-Haemolysin interaction with model membranes has been investigated by a 2-fold procedure. First, protein binding has been measured, by a direct method as well as through changes in the intrinsic fluorescence of the protein when incubated with liposomes and divalent cations. Then, the above results have been correlated with the protein lytic activity. The extent of protein binding is not significantly modified by the presence or absence of Ca2+, or by changes in lipid composition, although these factors influence greatly the membrane lytic activity of the protein. Moreover, Ca2+ binding to the toxin must occur prior to protein binding to the bilayer, for a lytic effect to take place.

Bacterial Proteins↗
PubMed1986

Effect of pH and energy spilling on bacterial protein synthesis by carbohydrate-limited cultures of mixed rumen bacteria.

Rumen contents were obtained from a cow fed 2.5 kg concentrates and 2.5 kg timothy hay twice daily, and the mixed rumen bacterial inoculum (pH 6.3) was separated from large feed particles and protozoa by centrifugation. Bacteria were incubated in artificial media at pH 6.7 and 6.0. When starch, sucrose, cellobiose, xylan, pectin, or a mix of carbohydrates were provided to pH 6.7 incubations at 1 mM/h for 10 h, fermentation was carbohydrate-limited, less than 20% of the carbohydrate was converted to lactate, molar ratio of methane to hexose fermented was as great as 49%, and pH remained constant. When initial pH was lowered to 6.0, methane production was nearly eliminated, volatile fatty acid production was reduced, and there was a small decrease (less than .5) in final pH. At pH 6.0, lactate production was increased in all incubations except xylan and pectin, and pH had a greater effect on acid production than the type of carbohydrate provided. Bacterial protein synthesis was reduced 34 to 69% when initial pH was 6.0, but these reductions were greater than decreases in carbohydrate utilization, increases in lactate, and associated decreases in adenosine 5'-triphosphate production. Because less adenosine 5'-triphosphate was used for protein synthesis, it appeared that low pH diverted energy to nongrowth functions.

Animals↗
PubMed2004

Direct bacterial protein PAMP recognition by human NK cells involves TLRs and triggers alpha-defensin production.

Although human CD56(+)CD3(-) natural killer (NK) cells participate in immune responses against microorganisms, their capacity to directly recognize and be activated by pathogens remains unclear. These cells encode members of the Toll-like receptor (TLR) family, involved in innate cell activation on recognition of pathogen-associated molecular patterns (PAMPs). We therefore evaluated whether the 2 bacterial protein PAMPs, the outer membrane protein A from Klebsiella pneumoniae (KpOmpA) and flagellin, which signal through TLR2 and TLR5, respectively, may directly stimulate human NK cells. These proteins induce interferon-gamma (IFN-gamma) production by NK cells and synergize with interleukin-2 (IL-2) and proinflammatory cytokines in PAMP-induced activation. Similar results were obtained using CD56(+)CD3(+) (NKR-expressing) T cells. NK cells from TLR2(-/-) mice fail to respond to KpOmpA, demonstrating TLR involvement in this effect. Defensins are antimicrobial peptides expressed mainly by epithelial cells and neutrophils that disrupt the bacterial membrane, leading to pathogen death. We show that NK cells and NKR-expressing T cells constitutively express alpha-defensins and that KpOmpA and flagellin rapidly induce their release. These data demonstrate for the first time that highly purified NK cells directly recognize and respond to pathogen components through TLRs and evidence defensins as a novel and direct cytotoxic pathway involved in NK cell-mediated protection against microorganisms.

Animals↗