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At least 19 recordsLinked to original sources
PubMed1985

Comparison of API 20E, API rapid E, and API rapid NFT for identification of members of the family Vibrionaceae.

Sixty isolates, from nine species of the family Vibrionaceae, were tested by the API 20E, API Rapid E, and API Rapid NFT systems. Results were compared with those obtained with standard biochemicals. Included were 7 Aeromonas caviae isolates, 27 Aeromonas hydrophilia isolates, 10 Aeromonas sobria isolates, 3 Plesiomonas shigelloides isolates, 3 Vibrio alginolyticus isolates, 3 Vibrio cholerae isolates, 1 Vibrio fluvialis isolate, 5 Vibrio parahaemolyticus isolates, and 1 Vibrio vulnificus isolate. The API 20E correctly identified all the isolates within 24 h. The API Rapid E correctly identified only 77%, misidentified 8%, and failed to identify 2% of the isolates in 4 h. The remaining 13% of the isolates gave a low selectivity identification, with one of the choices being correct. The API Rapid NFT correctly identified 87%, misidentified 5%, gave a low selectivity identification for 8% of the isolates, and in some instances, required up to 48 h of incubation. The API 20E is a valid system for use in the identification of the more commonly occurring members of the family Vibrionaceae and the most accurate and efficient of the three systems tested.

Reagent Kits, Diagnostic↗
PubMed1988

Enzymatic characterization of three aeromonas species using API Peptidase, API "Osidase," and API Esterase test kits.

An enzymatic characterization of 16 strains of Aeromonas species including A. hydrophila (7), A. sobria (5), and A. caviae (4) was carried out using API Peptidase (strips numbered 1, 2, 3, 4, 5, and 6); API Esterase and API "Osidase" test strips. A total of 89 substrates was used in the assay and included 59 arylamides (aminopeptides), 10 esters, and 20 carbohydrates. All three species were remarkably uniform in their reactivities. Nineteen (32%) of the arylamide substrates used were hydrolyzed by all three species. Very strong arylamidase activity was displayed by all three species for L-lysine, L-hydroxyproline, L-arginine, L-alanine, L-proline, and L-leucyl-L-alanine. Esterase activity was strongest against caproate (C6), caprylate (C8), nonanoate (C9), and caprate (C10) substrates. Only a limited number of carbohydrate substrates were hydrolyzed; strong N-acetyl-beta-D-glucosaminidase activity was given by all strains. Both A. hydrophila and A. caviae gave strong beta-D-glucosidase reactivities, while A. sobria appeared to be negative for this enzyme. The results of our preliminary study show that some of the enzymes examined may be useful in the identification and differentiation of these species. The API enzyme assays yielded rapid (4 hr) results. The assays were easy to perform, relatively inexpensive and reproducible. The importance of replicate testing and the inclusion of uninoculated (buffer only) controls as part of the assay is emphasized.

Aeromonas↗
PubMed1988

Comparison of API ZYM system with API AN-Ident, API 20A, Minitek Anaerobe II, and RapID-ANA systems for identification of Clostridium difficile.

The API ZYM system was compared with four anaerobe identification systems for the definitive identification of Clostridium difficile by using 88 cultures of C. difficile grown on Mueller-Hinton blood agar medium. The API ZYM system yielded a distinct and consistent enzyme profile for all test strains, whereas the sensitivities of the other systems in identifying C. difficile ranged from 78 to 96% (AN-Ident, 77.9%; RapID-ANA, 88.6%; Minitek Anaerobe II, 90.9%; and API 20A, 95.5%). The API ZYM system is highly reliable in identifying C. difficile accurately, is rapid, and is relatively simple to use.

Bacteriological Techniques↗
PubMed1977

API computer profiles: correlation of API 20E with API 10S.

A comparison of identifications of 201 clinical isolates with the 21-test API 20 Enteric kit and the subset of tests in API 10S indicated 85.6% agreement at the species level and 93.5% agreement at the genus level.

Bacteriological Techniques↗
PubMedDate not supplied

Characterization of aPY-like peptides in anglerfish brain using a novel radioimmunoassay for aPY-Gly.

Anglerfish peptide YG (aPY) was isolated from pancreatic islets of the anglerfish. Subsequent immunohistochemical and biochemical analyses demonstrated that anglerfish islet cells synthesize aPY. We have now developed and characterized a radioimmunoassay (RIA) for aPY and have examined extracts of anglerfish brain for aPY-like peptides. Brain extracts were subjected to gel filtration and high performance liquid chromatography (HPLC). Fractions from HPLC eluates were analyzed in the aPY RIA and also in a neuropeptide Y (NPY) RIA. A single peak of aPY-like immunoreactivity eluted from HPLC columns. The elution position of this aPY-like peptide coincided exactly with the aPY-Gly marker under several gradient conditions. Results from the NPY RIA confirmed the presence of several molecular forms of NPY-like immunoreactive peptides in the anglerfish brain. These results demonstrate the utility of the newly developed aPY RIA for studies of anglerfish brain peptides and extend our previous immunohistochemical demonstration of aPY-like staining in the anglerfish brain.

Animals↗
PubMed1987

Evaluation of a conventional routine method for identification of clinical isolates of coagulase-negative Staphylococcus and Micrococcus species. Comparison with API-Staph and API-Staph-Ident.

A collection of 138 consecutive isolates from blood primarily identified as Gram-positive, cluster-forming, coagulase-negative cocci was examined by a conventional routine method for identification of clinical isolates of coagulase-negative Staphylococcus and Micrococcus species. The method was based on selected reactions from the Kloos & Schleifer scheme, utilizing the conventional media of Statens Seruminstitut. Double determinations for each isolate were performed by the conventional method. The results were compared with speciation by the commercial micromethods API-Staph and API-Staph-Ident. For control, 31 Staphylococcus and 13 Micrococcus reference strains were included. Of the 31 Staphylococcus spp. (reference strains), the conventional system, API-Staph, and API-Staph-Ident correctly identified 87%, 87% and 81%, respectively. Micrococcus spp. were only identified to genus level by the conventional method as well as by API-Staph. API-Staph-Ident is not designed for Micrococcus identification. Of 138 blood isolates, 121 belonged to the genus Staphylococcus while 17 were Micrococcus spp. S. epidermidis dominated with all three methods, constituting approx. 35% of the isolates tested. In only 57% of the isolates identification by all three methods agreed. The three methods were unable to put a name on 7.5% (conventional method), 10.7% (API-Staph) and 2.5% (API-Staph-Ident) of the isolates. Reproducibility was high with the conventional method (100% for the reference strains and 91% for blood culture isolates) as well as with API-Staph and API-Staph-Ident (88%/81% and 81%/81%, respectively). We concluded that our conventional system was able to identify most clinically significant staphylococcal species by means of relatively few tests with a high certainty and a high degree of reproducibility.

Bacteriological Techniques↗
PubMed1985

Comparison of the API rapid E four-hour system with the API 20E overnight system for the identification of routine clinical isolates of the family Enterobacteriaceae.

Four hundred forty-one clinical isolates of the family Enterobacteriaceae were identified in parallel by using the API Rapid E 4-h and the API 20E overnight procedures (Analytab Products, Plainview, N.Y.). The results obtained by using the API Rapid E were compared with those obtained by using the API 20E. Discrepancies were resolved by using standard biochemicals. The API 20E identified 98.9% (436 of 441) of the isolates without the use of additional biochemicals and was found to be correct in each case of a discrepancy among the 436 isolates. The API Rapid E gave the same identification as the API 20E for 94.0% (410 of 436) of the isolates, misidentified 3.0% (13 of 436), and gave a correct but low-selectivity answer for the remaining 3.0% (13 of 436). The API Rapid E is a suitable alternative for the rapid identification of the Enterobacteriaceae.

Bacteriological Techniques↗
PubMed1985

API ZYM and API An-Ident reactions of fastidious oral gram-negative species.

API ZYM and API An-Ident enzymatic substrate tests were done on six oral species which are difficult to characterize with conventional biochemical tests. "Bacteroides forsythus, the "fusiform" Bacteroides species (A. C. R. Tanner, M. A. Listgarten, M. N. Strzempko, and J. L. Ebersole, manuscript in preparation), is difficult to cultivate in broth media, yet it gave 15 positive tests in these series. The tests were able to separate this new species from species of Capnocytophaga and Fusobacterium. "B. forsythus" reactions were similar but not identical to those of reference Bacteroides species. Positive reactions for alpha-glucosidase, beta-glucosidase, alpha-fucosidase, and alpha-glucuronidase suggest that "B. forsythus" may be saccharolytic. It was the only species tested which was trypsin positive. Wolinella species, Campylobacter concisus, B. gracilis, and Eikenella corrodens are asaccharolytic, and characterization relies heavily on sensitivities to inhibitory agents. These species reacted weakly in the API ZYM and API An-Ident enzymatic substrate tests, and the reactions were not useful for separating these species. The enzyme reactions differentiated Wolinella recta and C. concisus from Selenomonas sputigena, another oral motile but saccharolytic organism.

Bacteroidaceae↗
PubMed2026

Whole-genome sequences of the dwarf honey bee subgenus Micrapis: Apis andreniformis and Apis florea.

The Micrapis subgenus, which includes the black dwarf honey bee (Apis andreniformis) and the red dwarf honey bee (Apis florea), remains underrepresented in genomic studies despite its ecological significance. Here, we present high-quality de novo genome assemblies for both species, generated using a hybrid sequencing approach combining Oxford Nanopore Technologies long reads with Illumina short reads. The final assemblies are highly contiguous, with contig N50 values of 5.0 Mb (A. andreniformis) and 4.3 Mb (A. florea), representing a major improvement over the previously published A. florea genome. Genome completeness assessments indicate high quality, with BUSCO scores exceeding 98.5% using the Hymenoptera database and k-mer analyses supporting base-level accuracy. Repeat annotation revealed a relatively low repetitive sequence content (∼6%), consistent with other Apis species. Using RNA sequencing data, we annotated 12,189 genes for A. andreniformis and 12,207 genes for A. florea, with ∼98% completeness in predicted proteomes. These genome assemblies provide a valuable resource for comparative and functional genomic studies, with the potential to offer new insights into the genetic basis of dwarf honey bee adaptations.

Male↗
PubMed2026

Species-specific structuring of gut bacterial and fungal communities in honey bees Apis cerana and Apis mellifera.

Honey bee gut microbiome studies have primarily emphasized bacteria, leaving fungal communities comparatively overlooked despite their ecological and functional importance. Whole-genome shotgun metagenomics of Apis cerana and Apis mellifera revealed fungal assemblages dominated by Ascomycota, with Basidiomycota and Microsporidia in minor proportions, alongside gut bacterial communities composed mainly of Pseudomonadota, Bacillota, and Actinomycetota. The bacterial diversity was markedly higher in A. mellifera (Shannon = 5.90; Simpson = 0.98) than in A. cerana (Shannon = 4.01; Simpson = 0.94; p > 0.05), while fungal diversity remained comparable between species (p > 0.05). Beta-diversity analyses revealed strong host-specific clustering for both bacterial (PERMANOVA R2 = 0.7989, p > 0.05) and fungal communities (R2 = 0.7218, p > 0.05), indicating distinct microbial organization driven by host species. Bacterial-fungal co-occurrence patterns exhibited host-specific structuring, suggesting differential inter-kingdom community organization between A. cerana and A. mellifera. Linear Discriminant Analysis Effect Size (LEfSe) identified 93 discriminatory fungal taxa (45 enriched in A. cerana, 48 in A. mellifera), highlighting yeast-dominated signatures in A. mellifera and Basidiomycota-affiliated enrichments in A. cerana. KEGG and CAZy profiling revealed host- and kingdom-specific functional differences, with bacterial communities of A. mellifera showing distinct representation of carbohydrate metabolism and nutrient-cycling functions, while fungal communities exhibited a comparatively narrower functional repertoire. Together, these findings provide a high-resolution view of honey bee bacterial and fungal microbiomes, highlighting strong host-driven divergence in taxonomy, function, and cross-kingdom interactions.

Animals↗
PubMed1988

In vitro immunological degranulation of human basophils is modulated by lung histamine and Apis mellifica.

1. The effect of high dilutions of two homeopathic drugs Lung histamine (Lung his) and Apis mellifica (Apis mel) used for the treatment of allergic diseases has been assessed on in vitro human basophil degranulation. Experiments were conducted blind. 2. Basophil degranulation induced by 1.66 X 10(-9) M anti-IgE antibody was significantly inhibited in the presence of 5 Lung his (5th centesimal dilution of Lung his) and 15 Lung his (15th centesimal dilution of Lung his) by 28.8% and 28.6% respectively and by 65.8% in the presence of 9 Apis mel (9th centesimal dilution of Apis mel). Basophil degranulation induced by 1.66 X 10(-16) to 1.66 X 10(-18) M anti-IgE antibody was also inhibited by high dilutions of Lung his and Apis mel with an inhibition of nearly 100% with 18 Lung his (18th centesimal dilution of Lung his) and 10 Apis mel (10th centesimal dilution of Apis mel). An alternance of inhibition, inactivity and stimulation was observed when basophils were incubated in the presence of serial dilutions of Lung his and Apis mel. 3. The investigation of the clinical efficacy of high dilutions of Lung his and Apis mel should be envisaged in allergic diseases in parallel with in vitro and ex vivo biological assays.

Animals↗
PubMedDate not supplied

Glycine-extended anglerfish peptide YG (aPY) a neuropeptide Y (NPY) homologue may be a precursor of a biologically active peptide.

The 37 residue peptide YG (aPY), isolated from anglerfish endocrine pancreas, bears distinct sequence homology to the pancreatic polypeptide family of hormones. However, instead of a carboxyl-terminal tyrosine-amide, aPY has a free carboxyl-terminus ending with glycine. Towards studying the structure-activity relationship of this hormone, we have synthesized aPY by solid phase methodology using Boc-amino acid derivatives and phenylacetamidomethyl resin. The crude peptide was purified to homogeneity in 20% yield by reversed phase chromatography. The purified peptide had the expected amino acid composition and sequence, and was found to be identical with the natural aPY by analytical HPLC and peptide mapping of proteolytic digests. Neither the snythetic nor the natural aPY exhibited the characteristic vasoconstrictor activity of the related pancreatic polypeptide family of hormones. However, [Des37-Gly]-aPY, isolated from the anglerfish pancreas, caused vasoconstriction in rats. Based on these results and by analogy to the glycine-extended gastrin peptides, it may be suggested that aPY is a precursor of a biologically active peptide, namely [Des37-Gly]-aPY-amide.

Amino Acid Sequence↗
PubMed1991

Immunoreactivity to peptides belonging to the pancreatic polypeptide family (NPY, aPY, PP, PYY) and to glucagon-like peptide in the endocrine pancreas and anterior intestine of adult lampreys, Petromyzon marinus: an immunohistochemical study.

Immunoreactivity of antisera directed against human neuropeptide Y (NPY), anglerfish polypeptide YG (aPY), bovine pancreatic polypeptide (bPP), salmon pancreatic polypeptide (sPP), porcine peptide tyrosine tyrosine (PYY), and salmon glucagon-like peptide (GLP) was investigated in the endocrine pancreas and anterior intestine of adult lampreys, Petromyzon marinus, by immunohistochemical analysis. There was no immunoreactivity to anti-sPP and anti-bPP in any tissue and anti-GLP immunostaining was only present in the anterior intestine. The immunoreactivity to antisera raised against NPY, aPY, and PYY was colocalized within the same small number of cells in the caudal and cranial pancreas of juveniles and the caudal pancreas of upstream migrant adults. These antibodies did not immunostain B- or D-cells and thus, NPY, aPY, and PYY were likely localized in a third cell type (3a) in the lamprey pancreas. Immunostaining of a few cells with only anti-aPY suggested the possibility of a fourth cell type (3b). Immunoreactivity was similar in the cranial and caudal pancreas of male upstream migrants; however, in the female cranial pancreas, a few cells demonstrated intense immunoreaction to anti-aPY, while weaker immunostaining with this antiserum was observed in B-cells. In the intestine of juvenile and upstream migrant lampreys, positive immunostaining to GLP, NPY, aPY, and PYY antibodies was colocalized within the same cell. We believe that this cell may contain PYY/glucagon family peptides. Other intestinal cells immunostained with either GLP or somatostatin-34 antiserum.

Amino Acid Sequence↗
PubMed1992

Reevaluation of the API 20E identification system versus conventional biochemicals for identification of members of the family Enterobacteriaceae: a new look at an old product.

The API 20E bacterial identification system has been used for 19 years, often as the standard with which other identification systems are compared. Because the accuracy of this system compared with conventional biochemical tests has not been determined in many years, we evaluated the API 20E linear strip by using 291 typical and atypical strains of the family Enterobacteriaceae taken from a culture collection. At 24 h, the API 20E correctly identified by genus and species 229 of 291 (78.7%) of the strains, using Salmonella and Shigella serotyping where indicated. At 48 h, 95.2% were correctly identified by using additional biochemical tests as recommended by the manufacturer. The API 20E misidentified eight (2.7%) strains; these strains were not limited to any particular genus. When 81 of these Enterobacteriaceae strains were arranged into a weighted assortment correlating to the frequency with which they might be found in a clinical laboratory, the API 20E correctly identified 71 (87.7%) at 24 h and 78 (96.3%) at 48 h. This evaluation concluded that the accuracy of the identification of Enterobacteriaceae strains at 24 h (78.7%) may be significantly lower than that of earlier evaluations. However, there is no significant difference in the ability of the API 20E to correctly identify "challenge" type organisms (229 of 291) versus routine hospital isolates (71 of 81) (P greater than 0.05), but the system is not as accurate as the conventional biochemical method of identification.

Bacterial Typing Techniques↗