Immunological cross-reactivity and sequence homology between salivary proline-rich proteins in human and macaque monkey (Macaca fascicularis) parotid saliva

1979 ◽  
Vol 24 (8) ◽  
pp. 595-599 ◽  
Author(s):  
F.G. Oppenheim ◽  
E. Kousvelari ◽  
R.F. Troxler
Keyword(s):  
Sequence Homology ◽  
Macaca Fascicularis ◽  
Macaque Monkey ◽  
Cross Reactivity ◽  
Parotid Saliva

scholarly journals Bone biomarkers in koalas: validation of assays and preliminary analyses

2020 ◽  
Vol 32 (6) ◽  
pp. 856-863
Author(s):  
Chien-Jung Chen ◽  
Stephen T. Anderson ◽  
Natasha Steiger ◽  
Allan McKinnon ◽  
Joerg Henning ◽  
...  
Keyword(s):  
Sequence Homology ◽  
Population Decline ◽  
Traumatic Injury ◽  
Cross Reactivity ◽  
Bone Biomarkers ◽  
Normal Bone ◽  
Human Enzyme ◽  
High Incidence ◽  
High Sequence Homology ◽  
Bone Physiology

Traumatic injury, including bone fracture, is, to date, one of the leading causes of koala mortality in the South East Queensland region of Australia. Further, the specialist diet of koalas, which is restricted to certain Eucalyptus spp., may impact their normal bone physiology. Considering the dramatic koala population decline and high incidence of trauma, a greater understanding of koala bone physiology may support conservation. We retrieved from GenBank the protein sequences of parathyroid hormone (PTH), osteocalcin (OCN), and tissue-nonspecific alkaline phosphatase (TNALP) in human, dog, cattle, horse, koala, and gray short-tailed opossum. After homology was determined, plasma samples from 13 koalas were analyzed with human PTH, OCN, and bone-specific ALP (BALP) assay kits. Although koala PTH exhibited relatively low sequence homology with placental mammals, high sequence homology between humans and koalas was observed for both OCN and TNALP, and successful cross-reactivity was achieved using human enzyme immunoassay kits for detection of OCN and BALP biomarkers in koala plasma. However, we identified no correlation between OCN and BALP concentrations of healthy and trauma-affected koalas ( p = 0.66 and p = 0.79, respectively). Further analysis of OCN and BALP in healthy and diseased koalas will allow a better understanding of bone physiology in this unique marsupial.

THE IN VIVO METABOLISM OF CORTISOL AND CORTICOSTERONE BY THE MACAQUE MONKEY (Macaca fascicularis)

1975 ◽  
Vol 78 (1) ◽  
pp. 91-109 ◽  
Author(s):  
K. D. R. Setchell ◽  
C. H. L. Shackleton
Keyword(s):  
Mass Spectrometry ◽  
Gas Chromatography ◽  
Adult Female ◽  
Human Urine ◽  
Macaca Fascicularis ◽  
Macaque Monkey ◽  
The Other ◽  
Gas Chromatography Mass Spectrometry ◽  
In Vivo Metabolism

ABSTRACT [4-14C] Cortisol was administered intramuscularly to one adult female macaque monkey, MF3 (Macaca fascicularis). To adult female macaque monkey, MF4, [4-14C]corticosterone was administered intramuscularly. Urine samples were collected and the metabolites excreted identified using gas chromatography, radio-gas chromatography and gas chromatography-mass spectrometry. The principal metabolites of cortisol were identified as glucuronide conjugates of 11-oxygenated-17-oxosteroids. The excretion of tetrahydrocortisol and tetrahydrocortisone relative to the other corticosteroid metabolites was low compared with that of man. Two compounds, 3β-cortol and 3β-cortolone not normally present in human urine were identified in the urine from this species. The principal metabolites of corticosterone were glucuronide conjugates of hexahydroCompound A and hexahydrocorticosterone. Two unidentified radioactive compounds were also present.

Gustatory responses of single neurons in the insula of the macaque monkey

1990 ◽  
Vol 63 (4) ◽  
pp. 689-700 ◽  
Author(s):  
S. Yaxley ◽  
E. T. Rolls ◽  
Z. J. Sienkiewicz
Keyword(s):  
Macaca Fascicularis ◽  
Cynomolgus Macaque ◽  
Macaque Monkey ◽  
Solitary Tract ◽  
Single Neurons ◽  
Black Currant ◽  
Taste System ◽  
Basic Taste ◽  
Intensity Response ◽  
The Mean

1. In recordings made from 2,925 single neurons, a region of primary taste cortex was localized to the rostral and dorsal part of the insula of the cynomolgus macaque monkey, Macaca fascicularis. The area is part of the dysgranular field of the insula and is bordered laterally by the frontal opercular taste cortex. 2. The responses of 65 single neurons with gustatory responses were analyzed in awake macaques with the use of the taste stimuli glucose, NaCl, HCl, quinine HCl (QHCl), water, and black currant juice. 3. Intensity-response functions showed that the lowest concentration in the dynamic part of the range conformed well to human thresholds for the basic taste stimuli. 4. A breadth-of-tuning coefficient was calculated for each neuron. This is a metric that can range from 0.0 for a neuron that responds specifically to only one of the four basic taste stimuli to 1.0 for one that responds equally to all four stimuli. The mean coefficient for 65 cells in the taste insula was 0.56. This tuning is sharper than that of neurons in the nucleus of the solitary tract of the monkey, and similar to that of neurons in the primary frontal opercular taste cortex. 5. A cluster analysis showed that at least six different groups of neurons were present. For each of the taste stimuli, glucose, NaCl, HCl, QHCl, water, and black currant juice, there was one group of neurons that responded much more to that tastant than to the other tastants. Other subgroups of these neurons responded to two or more of these tastants, such as glucose and black currant juice, or NaCl and QHCl. 6. On the basis of this and other evidence, it is concluded that the primary insular taste cortex, in common with the primary frontal opercular taste cortex, represents a stage of information processing in the taste system of the primate at which the tuning of neurons has become sharper than that of neurons in the nucleus of the solitary tract, and is moving toward the fineness achieved in the secondary taste cortex in the caudolateral orbitofrontal taste cortex, where motivation-dependence first becomes manifest in the taste system.

scholarly journals Molecular Basis for Antigenic Variation of a Protective Strain-Specific Antigen of Ehrlichia risticii

1998 ◽  
Vol 66 (8) ◽  
pp. 3682-3688 ◽  
Author(s):  
Biswajit Biswas ◽  
Ramesh Vemulapalli ◽  
Sukanta K. Dutta
Keyword(s):  
Sequence Homology ◽  
Molecular Basis ◽  
Tandem Repeats ◽  
Antigenic Variation ◽  
Specific Antigen ◽  
Clinical Signs ◽  
Comparative Sequence Analysis ◽  
Cross Reactivity ◽  
Amino Acid Sequences ◽  
Ehrlichia Risticii

ABSTRACT Ehrlichia risticii, the causative agent of Potomac horse fever, has recently been isolated from many vaccinated horses with typical clinical signs of the disease. The heterogeneity of theE. risticii isolates obtained from the vaccinated horses necessitates the identification of the molecular basis of strain variations to elucidate the vaccine failure and to aid in the development of an efficient vaccine against this disease. As an attempt, two major cross-reacting surface antigen genes of 50- and 85-kDa antigens, present separately in strains 25-D (isolated in 1984) and 90-12 (isolated in 1990 from a vaccinated horse), respectively, were cloned and sequenced. A comparative sequence analysis revealed differences and similarities between these two antigens with strain-specific sizes (SSA). The 2.5- and 1.6-kb genes coding for the 85- and 50-kDa proteins, respectively, contained many different tandem repeats. The identical repeat motifs were more frequent in the middle of both genes, but the numbers and positions of the repeats were altogether different in the genes. Many of these direct repeats of both genes had exact sequence homology and coded for the same amino acids. The homology of the 5′- and 3′-flanking regions of the two genes was greater than that of the regions in the central part of the genes. A comparative analysis of the deduced amino acid sequences of these two antigen genes indicated eight common domains, which were designated identical domains. Although the sequence homologies of these identical domains were the same, the positions of the domains in their respective strains were completely different. This finding might be one of the bases of antigenic variation between the strains. In addition, there were a few unique regions in both antigen genes where no sequence homology existed. These specific regions were designated unique domains. The 50-kDa protein had two such unique domains, and the 85-kDa protein had six such unique domains. The presence of such unique domains contributed to the large size variation of these SSA. The cross-reactivity of recombinant proteins confirmed the presence of conserved epitopes between these two antigens. The SSA have been determined to be apparent protective antigens of E. risticii.

scholarly journals A common antigenic determinant found in two functionally unrelated toxins.

1984 ◽  
Vol 160 (4) ◽  
pp. 1253-1258 ◽  
Author(s):  
J Gariepy ◽  
P O'Hanley ◽  
S A Waldman ◽  
F Murad ◽  
G K Schoolnik
Keyword(s):  
Sequence Homology ◽  
Antigenic Determinant ◽  
Antigenic Site ◽  
Cross Reactivity ◽  
Homologous Region ◽  
Synthetic Analogs ◽  
E Coli ◽  
Heat Stable ◽  
Common Domain ◽  
Similar Conformation

The heat-stable enterotoxin ST Ib produced by enterotoxigenic E. coli strains shares a sequence homology with the sea snail neurotoxin, conotoxin GI. Rabbit antisera were raised against synthetic analogs of these toxins and to a six-residue peptide representing the region common to both toxins. Results from enzyme-linked immunosorbent assays indicate that the homologous region of both toxins represents part of their antigenic site. The lack of cross-reactivity exhibited by the six-residue common domain with serum directed against either toxin suggests that this region probably retains a similar conformation in the intact toxins but not in the isolated fragment.

scholarly journals Identification of Allergenic Component Tyr p 8 from Tyrophagus putrescentiae and Cross-Reactivity with Der p 8

2013 ◽  
Vol 20 (4) ◽  
pp. 506-512 ◽  
Author(s):  
En-Chih Liao ◽  
Yi-Hsueh Lin ◽  
Chih-Liang Chiu ◽  
Ting-Chu Lin ◽  
Jaw-Ji Tsai
Keyword(s):  
Sequence Homology ◽  
Positive Response ◽  
Specific Binding ◽  
Major Allergen ◽  
Specific Ige ◽  
Cross Reactivity ◽  
House Dust Mites ◽  
Tyrophagus Putrescentiae ◽  
Serum Samples ◽  
Content Type

ABSTRACTGroup 8 mite allergens exhibit sequence homology to glutathioneS-transferases (GSTs), such as that fromDermatophagoides pteronyssinus(Der p 8). GSTs have been identified as important allergens in studies of allergens from house dust mites, cockroaches, and fungi. Our objective was to purify the native group 8 allergen fromTyrophagus putrescentiae(nTyr p 8) and generate recombinant Tyr p 8 (rTyr p 8) for immunological characterization. The allergenicity was determined by antibody recognition, IgE inhibition, and triggering of the basophil-sensitized release of histamine, usingT. putrescentiaehypersensitivity sera. The results showed that the mRNA transcript of nTyr p 8 is 657 bp long, contains 218 amino acids with a molecular mass of 26 kDa, and exhibits 83% sequence homology to Der p 8. Serum samples from the allergic patients with an IgE-positive response toT. putrescentiaewere analyzed to determine their IgE response to rTyr p 8. The results showed that the sera of 48 subjects (45.3%) had specific IgE against rTyr p 8. However, sera of only 19 subjects (17.9%) had specific IgE against rTyr p 8 afterD. pteronyssinusabsorption. Histamine release was observed fromT. putrescentiae-allergic subjects in the presence of rTyr p 8. Both the nTyr p 8 andT. putrescentiaecrude extract had been demonstrated to possess GST enzymatic activity. Although the specific binding of serum IgE to rTyr p 8 was only 17.9%, which indicates that rTyr p 8 was not a major allergen, the positive response to rTyr p 8 was due to the cross-reactivity with Der p 8. The group 8 mite allergen might be of use in the design of a suitable allergen for diagnosis and for the development of novel immunotherapies.

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