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F Lopez-Bernad

Publications and source records attributed to F Lopez-Bernad.

5 recordsLinked to original sources

A method for the sequential study of eimerian chromosomes by light and electron microscopy.

In the present study, the authors describe a simple method to isolate chromosomes from eimerian oocysts and to submit them to sequential study by light and electron microscopy. This method includes a reliable and reproducible technique for transferring eimerian chromosomes from slides to grid that fulfills the essential requirements for generalized use in cytogenetics. In addition, this method overcomes the difficulty of the resistance of protozoan oocysts to disruption and permits the release of intact meiotic chromosomes. The observation by the authors of synaptonemal complexes in meiotic chromosomes of different Eimeria species by applying the above-mentioned method to oocysts revealed its importance to future applications.

Animals↗

Expression and localization of an S100 protein-like molecule in Eimeria tenella.

We investigated the expression of a calcium-binding protein, the S100 protein, in Eimeria tenella. Cecal paraffin sections from experimentally infected chickens were treated with anti-alpha-S100 (anti-alpha subunit of S100 protein) and anti-beta-S100 (anti-beta subunit of S100 protein) monoclonal antibodies and anti-S100 whole molecule polyclonal antibody. The avidin-biotin peroxidase method was used for immunocytochemical staining. Our results demonstrated a positive immunoreaction within the schizonts, macrogametes, and oocysts. These stages were all beta subunit and S100 whole-molecule positive. Immunoblot studies of the total proteins of E. tenella merozoites and sporozoites of the original strain and 2 precocious lines have demonstrated that precocious attenuation produced different S100 protein isotypes.

Animals↗

Identification of avian dendritic cells in the spleen using a monoclonal antibody specific for chicken follicular dendritic cells.

BACKGROUND: In the chicken, circulating antigens enter the splenic white pulp via the Schweigger-Seidel sheaths (ellipsoids), where they are bound by cells, the ellipsoid associated cells (EAC), which are located on the periphery of the ellipsoid. There is an increasing body of evidence that these antigen-binding cells move through the PALS, to be finally located within the germinal centers, where these antigen-transporting EAC function as follicular dendritic cells (FDC). The aim of the current study was to further study the relationship between the EAC, the FDC, and the antigen-bearing EAC which migrate through the splenic white pulp. METHODS: In order to identify the splenic FDC and their presumed migrating EAC precursors in the chicken, we used a monoclonal antibody produced against chicken FDC and an antiserum anti-S-100 protein which identifies chicken dendritic cells in lymphoid organs. RESULTS: Cells reacting with the 74.3 monoclonal antibody, which identifies FDC, were found within the germinal center, around the penicilliform capillary, in the periellipsoidal white pulp, and in the periarteriolar lymphatic sheaths (PALS). S-100+ cells were found in these same locations. CONCLUSIONS: A comparison between the staining patterns obtained with both antibodies strongly suggested that the intrasplenic distribution of 74.3+ cells was identical with that of FDC, EAC, and antigen-binding EAC migrating in the PALS. Therefore, the 74.3 monoclonal antibody identified not only FDC but also the splenic precursor cells of FDC, in accordance with the hypothesis of the migration of the EAC through the white pulp. S-100+ cells were more numerous than 74.3+ cells, which is in accordance with the fact that S-100 protein antibody stains both FDC and interdigitating dendritic cells (ID). This has allowed us to suggest that 74.3- EAC may represent precursors of ID. The current findings reinforce previous investigations, which provided evidence supporting the migration of EAC through the PALS and further supported the hypothesis which considers EAC precursors of FDC.

Animals↗

Identification of a fibronectin-like molecule on the surface of Leishmania amastigotes.

The major surface glycoprotein of Leishmania gp63, a fibronectin-like molecule, plays a key role in parasite-macrophage interaction. In this article, we describe a cross-reactivity between an anti-fibronectin monoclonal antibody and the amastigote gp63 by means of immunoelectron microscopy and immunoblot. Immunoreactivity was found on the amastigote membrane and in the flagellar pocket. We suggest that gp63 may play a role in the protection and/or nutrition process of the parasite in the phagolysosomes of the macrophage.

Animals↗

Identification of a fibronectin-like molecule on Eimeria tenella.

The attachment of Eimeria tenella to its target cells as an obligatory intracellular pathogen is essential for the development of disease. Previous reports have established that other intracellular protozoa parasites have either fibronectin, an adhesion protein, or fibronectin receptors, both of which are involved in the interaction with the host cells. In this current research, studies have been undertaken to visualize a surface component that may be involved in the attachment of E. tenella to host cells. For this purpose, monoclonal antibodies, both anti-chicken and anti-human fibronectin, and also anti-chicken integrin were used. Our results show a fibronectin-like molecule with an apparent molecular weight of 110 kDa in mature schizonts and microgametes. Staining with serum directed against chicken integrin revealed immunoreactivity within mature schizonts. Both the fibronectin-like molecule and the integrin may play an important role in the parasite stage-cell interaction and the promotion of parasite uptake.

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