46 research outputs found

    The parental care behaviour of Paratilapia polleni (Perciformes, Labroidei), a phylogenetically primitive cichlid from Madagascar, with a discussion of the evolution of maternal care in the family Cichlidae

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    The parental behaviour of the Madagascan cichlid, Paratilapia polleni , was studied in the laboratory. According to current hypotheses of phylogenetic intrarelationship for the family Cichlidae, Paratilapia is a representative of a phylogenetically primitive cichlid lineage, and as such is of particular interest in comparative evolutionary studies. Given the basal phylogenetic placement of Paratilapia it seems reasonable to expect that, if maternal participation in brood care arose within the extant Cichlidae, then the proposed plesiomorphic system of extensive male care of eggs and embryos may be retained in this taxon. This is not the case, and already by the fertilized-egg interval male and female roles in Paratilapia are strongly differentiated with the female as the primary care giver. In addition to specialized behavioural roles, a unique egg morphology and mobile egg mass is described for Paratilapia . The results of the study are discussed in the context of theories of the evolution of maternal brood care within the Cichlidae.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/42636/1/10641_2004_Article_BF00004768.pd

    Magnetic Compton scattering study of the ferromagnetic amorphous alloys Fe1-xBx

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    The boron contribution to the total spin moment in the amorphous alloys Fe1-xBx (x=0.2,0.24) has been determined using magnetic Compton scattering. The magnitude of the induced boron moment was found to be ≈-0.04μB per formula unit which is a factor of ≈2 less than that suggested by supercell linearized muffin-tin orbital electronic structure calculations. © 2001 The American Physical Society

    Characterization of the hepatitis C virus E2 epitope defined by the broadly neutralizing monoclonal antibody AP33

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    The mouse monoclonal antibody (MAb) AP33, recognizing a 12 amino acid linear epitope in the hepatitis C virus (HCV) E2 glycoprotein, potently neutralizes retroviral pseudoparticles (HCVpp) carrying genetically diverse HCV envelope glycoproteins. Consequently, this antibody and its epitope are highly relevant to vaccine design and immunotherapeutic development. The rational design of immunogens capable of inducing antibodies that target the AP33 epitope will benefit from a better understanding of this region. We have used complementary approaches, which include random peptide phage display mapping and alanine scanning mutagenesis, to identify residues in the HCV E2 protein critical for MAb AP33 binding. Four residues crucial for MAb binding were identified, which are highly conserved in HCV E2 sequences. Three residues within E2 were shown to be critical for binding to the rat MAb 3/11, which previously was shown to recognize the same 12 amino acid E2 epitope as MAb AP33 antibody, although only two of these were shared with MAb AP33. MAb AP33 bound to a panel of functional E2 proteins representative of genotypes 1-6 with higher affinity than MAb 3/11. Similarly, MAb AP33 was consistently more efficient at neutralizing infectivity by diverse HCVpp than MAb 3/11. Importantly, MAb AP33 was also able to neutralize the cell culture infectious HCV clone JFH-1. In conclusion, these data identify important protective determinants and will greatly assist the development of vaccine candidates based on the AP33 epitope
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