Pigeon and Dove Eggwhite Protect Mice Against Renal Infection Due to P Fimbriated Escherichia coli

Johnson, James R.; Berggren, Terriel

doi:10.1097/00000441-199405000-00004

Cited by 23 publications

(12 citation statements)

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“…The detailed structural studies of the major N-glycans presented here clearly indicate that the rich galabiose content is the reason the PEW glycoproteins serve as inhibitors for uropathogenic E. coli (23)(24)(25). Every oligosaccharide examined contain at least one and up to four galabiose sequences.…”

Section: Resultsmentioning

confidence: 82%

N-Glycan Structures from the Major Glycoproteins of Pigeon Egg White

Takahashi

Khoo

Suzuki

et al. 2001

Journal of Biological Chemistry

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N-Glycans from major glycoproteins of pigeon egg white (ovotransferrin, ovomucoid, and ovalbumins) were enzymatically released and were reductively aminated with 2-aminopyridine, separated, and structurally characterized by mass spectrometry and a three-dimensional mapping technique using three different columns of high performance liquid chromatography (HPLC) (Takahashi, N., Nakagawa, H., Fujikawa, K., Kawamura, Y., and Tomiya, N. (1995) Anal. Biochem. 226, 139 -146). Twentyfive major N-glycan structures, all of them hitherto unknown, were identified as pyridylamino derivatives. Of these, 13 were neutral, 10 were monosialyl, and 2 were disialyl oligosaccharides. All N-glycans contain from one to four Gal␣(1,4)Gal␤(1,4) sequences at the nonreducing terminal positions and are devoid of fucose residues. NAcetylneuraminic acids were ␣(2,6)-linked only to ␤-galactose. The HPLC profiles of the N-glycans from four different glycoproteins were qualitatively very similar to each other, but not identical in the peak distributions. Monosialyl glycans were most abundant in all four glycoproteins, followed by neutral glycans. Disialyl glycans were lowest in ovotransferrin, and highest in ovomucoid. Triantennary structures with bisecting GlcNAc were predominant in ovotransferrin, and tetra-antennary (with and without bisecting GlcNAc-containing) structures were predominant in other glycoproteins. Penta-antennary structures (with a sialic acid and without bisecting GlcNAc residue) were also found in small quantities in all four glycoproteins. In contrast to the chicken egg white counterparts, which contain mostly high mannose and hybrid types, all N-glycan structures in the major pigeon egg white glycoproteins are complex type.The presence of galabiose (Gal␣4Gal) sequence in N-glycans in any animal is only rarely noted. The only documented presence of such a sequence in N-glycan was that found in turtle dove ovomucoid (1, 2). The only other recorded presence of galabiose sequence were both in the O-glycosides found in the Chinese swiftlet nest (3) and in an insect cell line Mamestra brassicae clone SPCMb-92-C6 (4). As shown in the preceding paper (5), we have demonstrated that galabiose sequence is abundantly present in pigeon egg white (PEW) 1 glycoproteins, and it always occupies the terminal positions of the multiantennary structures. In the major N-glycans from the pigeon ovalbumin, no sialylation is found on the branch that contains the galabiose sequence. In contrast, chicken ovalbumin contained mostly high mannose type and hybrid types (6, 7) whereas chicken ovomucoid contains mostly galactose-less complex type (8). The preceding paper (5) also notes that, in contrast to the chicken and other avian egg whites hitherto investigated, the N-glycans in pigeon egg white glycoproteins seem to be more "mature," containing more of the multiantennary complex type structures. In view of these unique structural features, we felt that detailed structural studies were in order, not only to understand the underlying evolutionary sig...

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Section: Resultsmentioning

confidence: 82%

N-Glycan Structures from the Major Glycoproteins of Pigeon Egg White

Takahashi

Khoo

Suzuki

et al. 2001

Journal of Biological Chemistry

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“…In contrast, we found that pigeon egg white is a rich source of glycoproteins that possess the Gal␣1-4Gal␤1-4GlcNAc sequence at the nonreducing termini of N-glycans (4). It was demonstrated that pigeon egg white glycoproteins are useful in preventing infection with uropathogenic E. coli (7). We also found that the Gal␣1-4Gal sequence was absent from the egg white glycoproteins of two large taxa of avians, i.e.…”

mentioning

confidence: 77%

Molecular Cloning of Pigeon UDP-galactose:β-d-Galactoside α1,4-Galactosyltransferase and UDP-galactose:β-d-Galactoside β1,4-Galactosyltransferase, Two Novel Enzymes Catalyzing the Formation of Galα1–4Galβ1–4Galβ1–4GlcNAc Sequence

Suzuki

Yamamoto

2010

Journal of Biological Chemistry

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We previously found that pigeon IgG possesses unique N-glycan structures that contain the Gal␣1-4Gal␤1-4Gal␤1-4GlcNAc sequence at their nonreducing termini. This sequence is most likely produced by putative ␣1,4-and ␤1,4-galactosyltransferases (GalTs), which are responsible for the biosynthesis of the Gal␣1-4Gal and Gal␤1-4Gal sequences on the N-glycans, respectively. Because no such glycan structures have been found in mammalian glycoproteins, the biosynthetic enzymes that produce these glycans are likely to have distinct substrate specificities from the known mammalian GalTs. To study these enzymes, we cloned the pigeon liver cDNAs encoding ␣4GalT and ␤4GalT by expression cloning and characterized these enzymes using the recombinant proteins. The deduced amino acid sequence of pigeon ␣4GalT has 58.2% identity to human ␣4GalT and 68.0 and 66.6% identity to putative ␣4GalTs from chicken and zebra finch, respectively. Unlike human and putative chicken ␣4GalTs, which possess globotriosylceramide synthase activity, pigeon ␣4GalT preferred to catalyze formation of the Gal␣1-4Gal sequence on glycoproteins. In contrast, the sequence of pigeon ␤4GalT revealed a type II transmembrane protein consisting of 438 amino acid residues, with no significant homology to the glycosyltransferases so far identified from mammals and chicken. However, hypothetical proteins from zebra finch (78.8% identity), frogs (58.9 -60.4%), zebrafish (37.1-43.0%), and spotted green pufferfish (43.3%) were similar to pigeon ␤4GalT, suggesting that the pigeon ␤4GalT gene was inherited from the common ancestors of these vertebrates. The sequence analysis revealed that pigeon ␤4GalT and its homologs form a new family of glycosyltransferases.

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“…A well-established dual-strain (competition) model of unobstructed, atraumatic ascending UTI was used to compare the urinary tractcolonizing abilities of Ec1a and Ec1a⌬oxyRS and of Ec1a/pACYC184 and Ec1a⌬oxyRS/pACYC184oxyRS and to assess the impact of the p47 phoxϪ/Ϫ genotype on UTI outcomes (15,16,37,38,41,43). A competition model was used because this approach minimizes the impact of mouse-to-mouse variation and enhances sensitivity for detecting differences between test strains.…”

Section: Methodsmentioning

confidence: 99%

Effect of Inactivation of the Global Oxidative Stress Regulator oxyR on the Colonization Ability of Escherichia coli O1:K1:H7 in a Mouse Model of Ascending Urinary Tract Infection

2006

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To survive within the host urinary tract, Escherichia coli strains that cause urinary tract infection (UTI) presumably must overcome powerful oxidant stresses, including the oxygen-dependent killing mechanisms of neutrophils. Accordingly, we assessed the global oxygen stress regulator OxyR of Escherichia coli as a possible virulence factor in UTI by determining the impact of oxyR inactivation on experimental urovirulence in CBA/J and C57BL (both wild-type and p47 phox؊/؊ ) mice. The oxyR and oxyS genes of wild-type E. coli strain Ec1a (O1:K1:H7) were replaced with a kanamycin resistance cassette to produce an oxyRS mutant. During in vitro growth in broth or human urine, the oxyRS mutant exhibited the same log-phase growth rate (broth) and plateau density (broth and urine) as Ec1a, despite its prolonged lag phase (broth) or initial decrease in concentration (urine). The mutant, and oxyRS mutants of other wild-type ExPEC strains, exhibited significantly increased in vitro susceptibility to inhibition by H 2 O 2 , which, like the altered growth kinetics observed with oxyRS inactivation, were reversed by restoration of oxyR on a multiple-copy-number plasmid. In CBA/J mice, Ec1a significantly outcompeted its oxyRS mutant (by >1 log 10 ) in urine, bladder, and kidney cultures harvested 48 h after perurethral inoculation of mice, whereas an oxyR-complemented mutant exhibited equal or greater colonizing ability than that of the parent. Although C57BL mice were less susceptible to experimental UTI than CBA/J mice, wild-type and p47 phox؊/؊ C57BL mice were similarly susceptible, and the oxyR mutant of Ec1a was similarly attenuated in C57BL mice, regardless of the p47 phox genotype, as in CBA/J mice. Within the E. coli Reference collection, 94% of strains were positive for oxyR. These findings fulfill the second and third of Koch's molecular postulates for oxyR as a candidate virulence-facilitating factor in E. coli and indicate that oxyR is a broadly prevalent potential target for future preventive interventions against UTI due to E. coli. They also suggest that neutrophil phagocyte oxidase is not critical for defense against E. coli UTI and that the major oxidative stresses against which OxyR protects E. coli within the host milieu are not phagocyte derived.

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Pigeon and Dove Eggwhite Protect Mice Against Renal Infection Due to P Fimbriated Escherichia coli

Cited by 23 publications

References 23 publications

N-Glycan Structures from the Major Glycoproteins of Pigeon Egg White

N-Glycan Structures from the Major Glycoproteins of Pigeon Egg White

Molecular Cloning of Pigeon UDP-galactose:β-d-Galactoside α1,4-Galactosyltransferase and UDP-galactose:β-d-Galactoside β1,4-Galactosyltransferase, Two Novel Enzymes Catalyzing the Formation of Galα1–4Galβ1–4Galβ1–4GlcNAc Sequence

Effect of Inactivation of the Global Oxidative Stress Regulator oxyR on the Colonization Ability of Escherichia coli O1:K1:H7 in a Mouse Model of Ascending Urinary Tract Infection

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