Effects of broiler breeder genetic, diet type, and feeding program on maternal antibody transfer and development of lymphoid tissues in chicken progeny

Maternal antibody (MatAb) transfer is important for early chicken survivability. Diet composition and the amount of feed given to breeder pullets during rearing may affect the development of immunity and the transfer of MatAb to progeny, and could affect progeny performance and resistance to disease. The effects of broiler breeder nutrition and feeding management practices were evaluated for the transfer of MatAb to progeny and for spleen and bursa development at hatching in 2 genetic strains (A and B). In this experiment, the levels of MatAb against Newcastle disease virus were assessed by enzyme-linked immunosorbent assays in serum samples taken of pedigreed chicken progeny from hatching to 13 d of age. Chickens were fed corn-and wheat-based diets, as were their parents. The breeder feeding program and diet type altered the Newcastle disease virus MatAb found in progeny at hatching and affected how long these antibodies were maintained in circulation. Bursal follicle size at hatching was influenced by an interaction among all factors evaluated. Percentage of white pulp in the spleen was affected mainly by genetic strain and diet type, but responses varied according to the breeder feeding program. It was concluded that breeder feeding programs influence MatAb transfer and half-life, and may also affect the early development of lymphoid tissues.

Sensitive Affimer and Antibody Based Impedimetric Label-Free Assays for C-Reactive Protein

C-reactive protein (CRP) is an acute phase protein whose levels are increased in many disorders. Levels greater than 3 mu g/mL serum have hitherto been considered to indicate pathology, but there is increasing interest in assessments between 0.1 and 10 mu g/mL, which have been found to correlate with severity of risk for cardiovascular disease. We report herein the generation of both antibody and Affimer based impedance immunoassays for CRP that are substantially more sensitive than clinically utilized immunonephelometry and immunoturbidity assessments. Significant in this study is not only the use of a constrained peptide to detect a clinically important target but also that derived electrochemical impedance assays can be highly sensitive even with probes whose relatively weak (mu M) affinities are not amenable to target detection by surface plasmon resonance (SPR). Key to this finding is acknowledging that receptive surfaces of comparatively low initial steric bulk and charge transfer resistance are especially primed to be highly responsive to target binding in electroanalytical assays of this type.

Near-infrared Raman spectroscopy to detect anti-Toxoplasma gondii antibody in blood sera of domestic cats: quantitative analysis based on partial least-squares multivariate statistics

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Influence of HLA-DRB-1 alleles on the production of antibody against CSP, MSP-1, AMA-1, and DBP in Brazilian individuals naturally infected with Plasmodium vivax

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Rabbit antibody responses to experimental infestation with Dermatobia hominis.

The three larval stages of Dermatobia hominis (Linnaeus) have been evaluated for their immunogenicity by ELISA and immunodiffusion (ID) using sera from experimentally infested rabbits. During a primary infestation, first instar D. hominis were found to cause most reaction and allowed the earliest diagnosis by ELISA. An inhibition of the antibody response against second and third instars was observed. The inhibition disappeared after departure of the larvae from the host. In experimentally immunized hosts the antibody response, following challenge, was highest against second and third instar antigens. Antibody remained elevated during the infestation but fell immediately after the larvae had left the host.

Antibody response to the 43 kDa glycoprotein of Paracoccidioides brasiliensis as a marker for the evaluation of patients under treatment

Sera of patients with paracoccidioidomycosis contained IgG-, IgA-, and IgM-specific antibodies to a 43 kDa antigen contained in the filtrate of a culture of Paracoccidioides brasiliensis. IgG- and IgA-specific antibodies were present in all observed patients. The IgM response was more frequent in acute cases, and the mean titers of IgG- and IgM-specific antibodies were higher in the acute forms. By the fourth month of chemotherapy, there was a decay of IgG, IgA, and IgM antibody titers to this antigen in acute cases, correlating with clinical improvement. The detection of IgG and IgA antibodies and the sequential determination of antibodies to the 43 kDa glycoprotein may be useful tools for serodiagnosis and evaluation of therapeutic efficacy.

Characterization of myeloid or lymphoid acute leukemia by a chemiluminescence assay: Comparison with immunocytochemistry using an antimyeloperoxidase antibody

A simple and sensitive chemiluminescence assay for the demonstration of the activity of intracellular myeloperoxidase (MPO) is described, which is useful for the distinction between myeloid and lymphoid commitment in blasts from acute leukemia patients. When the cut-off point was settled at 13 mV of chemiluminescence all cases of acute myeloid leukemia (AML) were distinguished from those of acute lymphoid leukemia. In addition, this technique was able to demonstrate MPO activity in AML poorly differentiated (FAB-M0) which usually does not stain for MPO in classical cytochemistry preparations and could be negative also by immunocytochemistry with anti-MPO monoclonal antibody. Therefore the method here described presented a higher sensitivity than the immunocytochemistry procedure with anti-MPO.

U Pb and Sm Nd geochronologic studies of the eastern Borborema Province, Northeastern Brazil: initial conclusions

The Borborema Province of NE Brasil comprises the central part of a wide Pan-African-Brasiliano orogenetic belt that formed as a consequence of late Neoproterozoic convergence and collision of the São Luis-West Africa craton and the São Francisco-Congo-Kasai cratons. New Sm Nd and U Pb results from the eastern part of this province help to define the basic internal architecture and pre-collisional history of this province, with particular emphasis on delineating older cratonic terranes, their fragmentation during the Mesoproterozoic, and their assembly into West Gondwana during the Pan African-Brasiliano orogeny at ca. 600 Ma. The region can be divided into three major geotectonic domains: a) Rio Piranhas-Caldas Brandão massif, with overlying Paleoproterozoic to Neoproterozoic supracrustal rocks, north of the Patos Lineament; b) the Archean to Paleoproterozoic São Francisco craton (SFC) to the south; and c) a complex domain of Paleoproterozoic to Archean basement blocks with several intervening Mesoproterozoic to Neoproterozoic fold belts in the center (south of Patos Lineament and north of SFC). The northern and central domains comprise the Borborema Province. Archean basement gneiss and Transamazonian granulite of northern SFC are exposed in the southern part of the central domain, underlying southern parts of the Sergipano fold belt. Basement in the Rio Piranhas massif appears to consist mostly of Transamazonian (2.1 to 2.2 Ga) gneissic rocks; Nd model ages (TDM) of ca. 2.6 Ga for 2.15 Ga gneisses indicate a substantial Archean component in the protoliths to these gneisses. The Caldas Brandão massif to the east yields both Transamazonian and Archean U Pb zircon and Nd (TDM) ages, indicating a complex architecture. Metasedimentary rocks of the Jucurutu Formation yield detrital zircons with original crystallization ages as young as 1.8 Ga, indicating that these rocks may be late Paleoproterozoic and correlate with other ca. 1.8 Ga cratonic supracrustal rocks in Brazil such as the Roraima Group and Espinhaço Group. Most metavolcanic and pre-Brasiliano granitic units of the Sergipano (SDS), Pajeú-Paraíba (SPP), Riacho Pontal (SRP), and Piancó-Alto Brígida (SPAB) fold belts in the central domain formed ~ 1.0 ± 0.1 Ga, based on U Pb ages of zircons. Nd model ages (TDM) for these same rocks, as well as Brasiliano granites intruded into them and large parts of the Pernambuco-Alagoas massif, are commonly 1.3-1.7 Ga, indicating that rocks of the fold belts were not wholly derived from either older (> 2.1 Ga) or juvenile (ca. 1.0 Ga) crust, but include mixtures of both components. A simple interpretation of Brasiliano granite genesis and the Nd data implies that there is no Transamazonian or Archean basement underlying large parts of these fold belts or of the Pernambuco-Alagoas massif. An exception is a belt of syenitic Brasiliano plutons (Syenitoid Line) and host gneisses between SPAB and SPP that clearly has a Transamazonian (or older) source. In addition, there are several smaller blocks of Archean to Transamazonian gneiss that can be defined within and among these fold belts. These blocks do not appear to constitute a continuous basement complex, but appear to be isolated older crustal fragments. Our data support a model in which ca. 1.0 Ga rifting was an important tectonic and crust-forming event along the northern edge of the São Francisco craton. Our data also show that significant parts of the Borborema Province are not remobilized Transamazonian to Archean crust, but that Mesoproterozoic crust is a major feature of the Province. There are several small remnants of older crust within the area dominated by Mesoproterozoic crust, suggesting that the rifting event created several small continental fragments that were later incorporated into the Brasiliano collisional orogen. We cannot at present determine if the Rio Piranhas-Caldas Brandão massifs and the older crustal blocks of the central domain were originally part of the São Francisco craton or whether some (or all) of them came from more exotic parts of the Proterozoic Earth. Finally, our data have not yet revealed any juvenile terranes of either Transamazonian or Brasiliano age. © 1995.

Laminin-binding epitope on gp43 from Paracoccidioides brasiliensis is recognized by a monoclonal antibody raised against Staphylococcus aureus laminin receptor

Adhesion is regarded as an important step in the pathogenesis of several microorganisms. Thus, the ability to recognize extracellular matrix proteins, such as laminin or fibronectin, has been correlated with invasiveness. Studying the already characterized laminin-binding protein of Paracoccidioides brasiliensis, the 43 kDa glycoprotein (gp43), we evaluated whether MAb 1.H12, raised against the laminin-binding protein from Staphylococcus aureus, cross-reacts with that fungal protein. By immunoblot analysis we show that MAb 1.H12 recognizes gp43. This interaction is able to inhibit the laminin-mediated adhesion to epithelial cells as well as the P. brasiliensis infection in vivo. Moreover, through immunoenzymatic assays, we show that MAb 1.H12 recognizes gp43 in solid phase and that this interaction is partially inhibited by the addition of anti-gp43 MAbs. These results show that MAb 1.H12 recognizes the gp43, suggesting the presence of an epitope similar to those found in the other laminin-binding proteins from phylogenetically very distant cells. These findings reinforce the possibility of evolutionary conservation of such epitopes.

IgG, IgM and IgA antibody response for the diagnosis and follow-up of paracoccidioidomycosis: Comparison of counterimmunoelectrophoresis and complement fixation

IgG, IgM and IgA antibodies to GP43 (glycoprotein fraction of Paracoccidioides brasiliensis) were measured by ELISA in 63 samples from 23 patients with paracoccidioidomycosis before and twice after chemotherapy was started. Antibodies against P. brasiliensis were detected by indirect immunofluorescence (IF) (IgG, IgM and IgA isotypes), counterimmunoelectrophoresis (CIE) and complement fixation. Two control groups composed of 19 healthy individuals and 12 patients with other diseases (six with histoplasmosis, three with tuberculosis and three with other mycoses). The highest efficiency percentages were found with IgG and IgA- ELISA (100%), IgG-IF (96.2%), CIE (94.4%) and the lowest with CF (75.9%). Highest positive and negative predictive values (100%) were observed for IgG and IgA ELISA. IgG and IgM-ELISA antibodies are more often found in patients with acute than chronic disease (P = 0.01). Four to six months after treatment follow-up showed decreased levels of IgG and IgM-ELISA for acute cases and decreased titres of CIE for chronic cases in relation to pretreatment levels. This study suggests that IgG-ELISA anti-GP43 represents a good marker to monitor clinical response to therapy.

Characterization of a monoclonal antibody recognizing mast cells

Immunohistochemical screening for monoclonal antibodies prepared by immunization of mice with a rat osteoblastic cell population led to identification of one antibody that reacted against a small population of cells present in the soft connective tissue compartment of 21 days fetal rat calvaria. The morphology of the cells and the immunohistochemical staining characteristics (a distinct intracellular granular pattern) suggested that the antibody might be reacting specifically against mast cells. We used combined histochemistry and immunohistochemistry to further characterize this antibody, designated RCJ102. Cryosections containing calvaria bone, soft connective tissues and skin were prepared from the top of the head of 21 days fetal rats, and from adult rats cryosections of lung, muscle, adipose tissue and small intestine were prepared. Some sections were labelled by indirect immunofluorescence with RCJ102; corresponding sections were labelled histochemically with toluidine blue. There was a direct correspondence between mast cells identified histochemically and cells labelling with RCJ102 in all tissues except intestine, in which the mast cell detectable by histochemistry were not labelled by RCJ102. These results suggest that the RCJ102 antibody will be a valuable new reagent for further elucidation of the heterogeneity described between connective tissue and intestinal mucosal mast cells.