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At least 55 records · Page 3Linked to original sources
PubMed2005

Profiling differential gene expression of corals along a transect of waters adjacent to the Bermuda municipal dump.

A coral cDNA array containing 32 genes was used to examine the gene expression profiles of coral populations located at four sites that varied with distance from a semi-submerged municipal dump in Castle Harbour, Bermuda (previously identified as a point source of anthropogenic stressors). Genes on the array represent transcripts induced under controlled laboratory conditions to a variety of stressors both natural (temperature, sediment, salinity, darkness) and xenobiotic (heavy metals, pesticides, PAH) in origin. The gene expression profiles produced revealed information about the types of stressors. Consistent with other studies undertaken in Castle Harbour, the coral cDNA array detected responses to heavy metals, sedimentation, as well as oxidative stress.

Animals↗
PubMed1996

Employer-based health insurance and seniors: the case of Bermuda.

This article examines the importance of economic factors in physician and other health service utilization among older adults living in Bermuda. Using data drawn from a national survey of 500 Bermudian elders, the findings reveal economic factors to be unrelated to the use of physician services directly, but to be significant determinants of the use of other health services. Need plus non-need factors are related to the use of both physician and other health services. The employer-based system does seem to provide universal access, but factors in addition to need influence the receipt of care.

Aged↗
PubMed1978

A clinical environmental study of the aeroallergens of the islands of Bermuda.

The major allergen responsible for allergic respiratory disease in the islands of Bermuda has been shown to be derived from Dermatophagoides pteronyssinus. 73% of the atopic group included in the survey gave weal and erythema reactions to extracts of this mite, whereas only 30% reacted to mixed pollen extracts and 10% to mould extracts. D. pteronyssinus was isolated from all house dust samples and it represented nature, with only a modest seasonal influence, and pollen counts were low throughout the year.

Adolescent↗
PubMed1968

DDT residues and declining reproduction in the Bermuda petrel.

Residues of DDT [1,1,1-trichloro-2,2-bis(p-chlorophenyl)ethane] averaging 6.44 parts per million in eggs and chicks of the carnivorous Bermuda petrel indicate widespread contamination of an oceanic food chain that is remote from applications of DDT. Reproduction by the petrel has declined during the last 10 years at the annual rate of 3.25 percent; if the decline continues, reproduction will fail completely by 1978. Concentrations of residues are similar to those in certain terrestrial carnivorous birds whose productivity is also declining. Various considerations implicate contamination by insecticides as a probable major cause of the decline.

Animals↗
PubMed1980

Poxvirus infection of the white-tailed tropicbird (Phaethon lepturus) in Bermuda.

Lesions caused by an avian poxvirus were identified on the face and nares of fledgling white-tailed tropicbirds (Phaethon lepturus catesbyi) in the natural environment on Bermuda. Between 1958 and 1978, 6 of 81 fledglings found off the nest and unable to fly at departure time had lesions suggestive of poxvirus infection. More detailed nest-site surveys from 1974 to 1978 indicated an overall prevalence of less than 0.5%, involving the fledgling population only.

Animals↗
PubMed2005

Sub-proteome analysis of novel IgE-binding proteins from Bermuda grass pollen.

Bermuda grass (Cynodon dactylon) pollen (BGP) is one of the most common causes of airway allergic disease, and has been shown to contain over 12 allergenic proteins on 1-D immunoglobulin E (IgE) immunoblots. However, only a few allergens have been identified and characterized. Cyn d 1 is a major allergen and the most abundant protein in BGP, representing 15% of the whole-pollen extract. To investigate variability in the IgE-reactive patterns of BGP-sensitized patients and to identify other prevalent allergens, a BGP extract was passed through an affinity column to remove Cyn d 1, and the non-bound material was collected and analyzed by 2-DE. IgE-reactive proteins were subsequently characterized by immunoblotting using serum samples from ten BGP-allergic patients. The prevalent IgE-reactive proteins were identified by MALDI-TOF MS, N-terminal sequence similarity, and LC-MS/MS. Here, we present a sub-proteome approach for allergen investigation and its use for determining BGP 2-DE profiles and identifying six novel allergens.

Blotting, Western↗
PubMed2001

Structural characterization of the 60-kDa bermuda grass pollen isoallergens, a covalent flavoprotein.

Our studies suggest a tripartite structure for the 60-kDa allergen of Bermuda grass pollen (BG60) including a short N-terminal segment, a FAD-binding domain, and a C-terminal domain. The lower molecular weight isoallergens lack the N-terminal segment. The higher protease susceptibility and the lower melting temperature of approximately 20 degrees C of the lower molecular weight isoforms suggest that the N-terminal segment is essential for a compact structure. Database screening reveals that the protease-digested peptide sequences (approximately 180 residues in total) share 40% identity with the plant berberine bridge enzymes. In particular, a 24-residue peptide sequence displays high similarity to a conserved FAD-binding motif. The spectroscopic and SDS-PAGE analyses suggest that the cofactor FAD is covalently linked to the central domain. Therefore, we conclude that BG60 is identified as the first flavinylated allergen.

Allergens↗
PubMed1999

Crystallization and preliminary diffraction data of 60-kDa glycosylated pollen isoallergens from Bermuda grass.

Crystals grown from a 60-kDa isoallergen mixture of Bermuda grass pollen have been obtained in 30% PEG 4000 and 25% isopropanol. The crystals diffract beyond 2-A resolution and belong to a tetragonal space group with the unit cell dimensions a = b = 86 A and c = 310 A. The preferential crystal growth of the larger isoallergens with a blocked N-terminus indicates that crystallization can isolate proteins with compact conformation.

Allergens↗
PubMedDate not supplied

Purification and characterization of a novel isoallergen of a major Bermuda grass pollen allergen, Cyn d 1.

A novel immunoreactive isoallergen of a major Bermuda grass pollen allergen, Cyn d 1, was purified by the use of a combination of various chromatographic techniques, including high-performance liquid chromatography. This new isoallergen has a pI value of 9.1 and shows significant N-terminal sequence homology with other isoforms. Carbohydrate composition analysis revealed a 10.4% carbohydrate content consisting of 7 different sugar moieties, including arabinose, fucose, galactose, glucose, mannose, xylose and N-acetylglucosamine, as well as a trace amount of rhamnose. Upon periodate oxidation, the binding activities of the Cyn d 1 isoform to murine monoclonal antibodies and human serum IgE and IgG were reduced, suggesting the importance of the carbohydrate moiety in the immune response. The availability of the purified Cyn d 1 basic isoform will allow for further structural and immunological characterization, and ultimately for the design of an appropriate therapy.

Allergens↗
PubMed1994

A Common Allergenic Epitope of Bermuda Grass Pollen Shared by Other Grass Pollens.

The present study disclosed the cross-reactivity between Bermuda grass pollen (BGP) and other grass pollens using monoclonal antibodies (MAbs) and polyclonal antiserum. MAb 9-13, directed against a group of minor allergens of BGP (Cyn d Bd68K, 48K, 38K) was found to cross-react with extracts of ten other grass pollens. Immunoblotting assays illustrated that MAb 9-13 cross-reacted with multiple components of most of these pollens, and the major cross-reactive components had molecular weights of 29-36 kD. The crossreactivity between BGP and Lol pI, the group I allergen of rye grass pollen, was further evaluated; Lol pI was recognized by MAb 9-13, but not by our MAbs/polyclonal antiserum against Cyn dI, the major allergen of BGP. These results suggest that the epitope recognized by MAb 9-13 is a common (C) epitope shared by Lol pI and Cyn d Bd68K, 48K, 38K, and Cyn dI does not share significant antigenicity with Lol pI. In a modified radio-allergosorbent test, IgE antibodies in the serum of BGP-allergic patients reacted mildly with C-epitope-bearing components of both BGP and rye grass pollens, and this binding could be blocked specifically by MAb 9-13. This suggests that in addition to an antigenic cross-reaction, the C epitope can also lead to an allergenic cross-reaction. Copyright 1994 S. Karger AG, Basel

Journal Article↗
PubMedDate not supplied

Isolation and partial characterization of a 46-kd allergen of Bermuda grass pollen.

Cyn d Bd46K, a 46-kD component of Bermuda grass (Cynodon dactylon) pollen, had been identified as an allergenic constituent. In the present study two-dimensional (2D) gel electrophoresis illustrated the presence of five acidic isoforms in Cyn d Bd46K, and this molecule was purified by monoclonal antibody (MAb) affinity chromatography for further characterization. Using a digoxigenin-labeled lectin-binding assay, the elucidating protein was disclosed to be a glycoprotein with terminal mannose. The involvement of a carbohydrate moiety in the allergenicity and antigenicity of the elucidated molecule was demonstrated with sodium-periodate-treated Cyn d Bd46K, which reduced binding to its specific MAb and human IgE. We were unable to identify the N-terminal amino acid sequences of Cyn d Bd46K, but some internal amino acid sequences were disclosed by microsequencing some fragments cleaved by Achromobacter protease I and fractionated by reversed-phase column chromatography. The amino acid sequences of 4 identified Cyn d Bd46K internal peptide fragments were found to be 25-71% identical with that of cytochrome c oxidase III from corn grass pollen. The present study provided important information for future experiments on the molecular cloning of the elucidated allergen.

Allergens↗
PubMed1991

Characterization of the major allergen of Cynodon dactylon (Bermuda grass) pollen, Cyn d I.

An allergen from Cynodon dactylon (Bermuda grass) pollen, Cyn d I, has been purified by a combination of concanavalin A-Sepharose affinity chromatography, and carboxymethyl-Sepharose chromatography. The allergen constitutes the major allergenic component of the pollen extract as observed by immunoelectrophoretic techniques, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, an IgE-inhibition experiment, and skin testing. In sodium dodecyl sulfate-polyacrylamide gel electrophoresis, Cyn d I is presented as a dominant 32 kd band and a minor 29 kd band, both binding IgE. Both bands are identified by monospecific rabbit antibodies (Abs) raised against Cyn d I. These Abs only weakly precipitate allergens from other grass species, indicating that Cyn d I possesses some unique immunochemical properties. Two of four purified murine monoclonal Abs raised against Cyn d I also bind to both bands of Cyn d I, indicating that the bands represent isoallergens with slightly different immunochemical properties. All four monoclonal Abs cross-react with pollen components from other grass species, especially Poa pratensis and Dactylis glomerata. The NH2-terminal sequence corresponding to approximately 10% of the complete sequence was determined, and it revealed high homology to the corresponding sequence of the major allergen of Lolium perenne, Lol p I. From the amino acid composition determination and immunoelectrophoretic comparison, the amount of Cyn d I in the source whole-pollen extract was estimated to be 15% wt/wt.

Allergens↗
PubMed1993

Identification and characterization of epitopes on Cyn d I, the major allergen of Bermuda grass pollen.

BACKGROUND: We identified three epitopes on Cyn d I by using four anti-Cyn d I monoclonal antibodies (MoAbs). METHODS: In a cross-inhibition binding assay, the binding of MoAbs 1-61 and 10-7 to Cyn d I was completely blocked by each other but not by MoAbs 4-37 and 11-7; the binding of MoAb 4-37 and MoAb 11-7 to Cyn d I was inhibited by themselves but not by other MoAbs. The epitope recognized by MoAbs 1-61 and 10-7 is designated as E1, and those recognized by MoAbs 4-37 and 11-7 are designated as E2 and E3, respectively. RESULTS: In a radioallergosorbent inhibition assay, we found that MoAbs 1-61 and 4-37 (1:50 diluted) can inhibit the binding of human Immunoglobulin Es to Cyn d I by more than 30%, whereas MoAb 11-7 was less efficient (reduced by only 6%). These results suggest that both E1 and E2 are major allergenic epitopes but that E3 is only a minor one. Further characterization of E1 and E2 reveals that they are labile in alkaline but resistant to acid and sodium periodate treatments. Moreover, E1 is heat-labile, but guanidine- and urea-sensitive, whereas E2 is not. Both E1 and E2 lost their antigenicity after reduction and alkylation. CONCLUSIONS: Results of the present study provide important information on the physicochemical properties of major allergenic epitopes on Cyn d I, which may be useful for future development of therapeutic peptides for patients allergic to Bermuda grass pollen.

Allergens↗
PubMed2005

Historical and ecological analysis of coral communities in Castle Harbour (Bermuda) after more than a century of environmental perturbation.

The coral reefs in Bermuda's Castle Harbour basin have been subjected to varying anthropogenic stressors for over 100 years. These include restriction of water flow through the construction of a causeway in the late 19th century and an extensive dredging and land reclamation operation during World War II. In the 1970s, disposal of bulk waste commenced at a foreshore reclamation site in Castle Harbour. Since 1996 the waste stream has included blocks of cement-stabilized municipal incinerator ash. This study provides a historical and quantitative ecological review of the Castle Habour reef ecosystem as a case study, assessing the responses of the reef to more than a century of anthropogenic disturbance. Measures of the coral community, flow rates, turbidity and sedimentary regimes suggest the present structure of the coral community largely reflects the impacts of the historic dredge and fill operations prior to the establishment of the foreshore dump site. Recent increases in the abundance of some sediment tolerant, massive reef-building coral species (Diploria strigosa and Montastraea cavernosa) suggest adaptation to chronic sediment stress.

Adaptation, Physiological↗
PubMed1997

Molecular cloning and immunological characterisation of Cyn d 7, a novel calcium-binding allergen from Bermuda grass pollen.

A cDNA coding for a newly identified Bermuda grass pollen allergen, Cyn d 7, with significant sequence similarity to Ca2+-binding proteins, was isolated from a cDNA expression library using serum IgE from an allergic individual. The deduced amino acid sequence of Cyn d 7 contained two typical Ca2+-binding sites (EF hand domains). Depletion of Ca2+ with EGTA led to a loss of IgE-binding capacity of rCyn d 7. A synthetic peptide based on domain II showed high IgE reactivity. Cyn d 7 therefore represents a grass pollen allergen that belongs to a novel class of Ca2+-binding proteins.

Allergens↗
PubMed1996

Immunologic and physicochemical studies of Bermuda grass pollen antigen BG60.

BACKGROUND: In a previous study we showed that antigen BG60 of Bermuda grass pollen contains isoallergens. Because the yield of purified isoallergens was low when a chromatofocusing technique was used, it was difficult to carry out further studies, such as determination of carbohydrate composition and structure. OBJECTIVE: The aim of this study was to establish a procedure to purify antigen BG60 proteins as a group and to characterize this group's physicochemical and immunologic properties. METHODS: A combination of chromatographic techniques (ion-exchange, gel filtration, blue gel affinity, and reverse-phase high-performance liquid chromatography) was used for the purification of BG60. Immunoblot and ELISA techniques were used to study BG60-specific IgE and IgG antibodies in patients' sera. The role of the carbohydrate moiety in antigenicity and allergenicity was examined with monoclonal antibodies and allergic sera by using periodate-treated BG60. Its carbohydrate composition was analyzed by high-performance anion-exchange chromatography with a pulsed amperometric detector. RESULTS: Homogeneity of BG60 was demonstrated by a single sharp peak in reverse-phase high-performance liquid chromatography, a single band in sodium dodecylsulfate-polyacrylamide gel electrophoresis, and only one band stained by anti-BG60 monoclonal antibody. BG60-specific IgE and IgG antibodies were shown to be present in allergic sera. Six plant lectins were found to react with BG60. On periodate treatment, BG60 reduced binding toward its monoclonal antibody and human IgE and IgG. Carbohydrate composition analysis showed that BG60 contains three kinds of sugars: mannose, N-acetylglucosamine, and fucose (in a ratio of approximately 3:2:1) and a minute amount of xylose. The carbohydrate content is approximately 7.5%, and peptide content is about 92.5%. CONCLUSION: A procedure was established for the purification of a large quantity of the BG60 antigen. The results suggest that the carbohydrate moiety of antigen BG60 may play an important role in the immune response.

Allergens↗
PubMed2002

Sequence of the coat protein gene of Bermuda grass etched-line virus, and of the adjacent 'marafibox' motif.

The complete nucleotide sequence of the coat protein (CP) gene of Bermuda grass etched-line virus (BELV), including 376 nucleotides (nt) of the region to its 5' side, was determined and compared with sequences of the other viruses associated with the genus Marafivirus, substantiating the assignment of BELV to this group. The CP gene coding sequence was 585 nt in length. Inferred amino acid sequences showed homologies among marafiviral CP gene products ranging from 41% to 59%. A non-coding sequence motif characteristic of the marafiviruses lies in the region adjacent to the CP gene to the 5' side. In contrast to various homology levels in the coding regions of the CP genes, the interspecific sequence homology in this 18 nt motif was almost perfect.

Amino Acid Motifs↗
PubMed1996

The carbohydrate moiety of the bermuda grass antigen BG60. New oligosaccharides of plant origin.

BG60 is an important allergen of Bermuda grass (Cynodon dactylon) pollen, which causes allergic responses in human. It was suggested that its carbohydrate moiety may be relevant to allergic reaction (Su, S. N., Lau, G. X., Shu, P., Yang, S. Y., Huang, S. W., and Lee, Y. C. (1996) J. Allergy Clin. Immunol., in press). Therefore, the structure of the carbohydrate moiety in BG60 was investigated. The N-linked oligosaccharides were released from the glycopeptides of BG60 by digesting with a glycoamidase from sweet almond and reductively aminated with a fluorescent reagent, 2-aminopyridine. The mixture of pyridylaminated oligosaccharides were separated by high-performance liquid chromatography (HPLC) using an octadecylsilyl (ODS) column. Five oligosaccharide fractions were isolated, and each fraction was found to be homogeneous by HPLC on an amide-silica column. The structure of each of the oligosaccharides was analyzed by the two-dimensional mapping technique (Tomiya, N., Awaya, J., Kurono, M., Endo, S., Arata, Y., and Takahashi, N. (1988) Anal. Biochem. 171, 73-90), in tandem with sequential exoglycosidase digestion. The two most abundant oligosaccharides, A and B, have an unusual structural feature, i.e. the presence of an L-Fuc alpha-(1,3)-linked to Asn-linked GlcNAc without a Xyl beta-(1,2)-linked to the branching Man (see below). To the best of our knowledge, these are the first such oligosaccharides found in plant glycoproteins.

Allergens↗