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Showing papers by "Fanny Guzmán published in 1991"


Journal Article
TL;DR: It was found that the peptides could be grouped, according to their RBC-binding kinetics, into high, medium and low binding activity, and a direct correlation was detected between a peptide's binding activity and inhibitions of human RBC reinvasion.
Abstract: In the search for strategies which might help in the elucidation of molecular mechanisms involved in the red blood cell (RBC) invasion by P. falciparum merozoites, and with the specific aim of establishing whether synthetic peptides derived from selected parasite proteins bind to human RBCs, 26 different peptides were chemically synthesized and radiolabeled. It was found that the peptides could be grouped, according to their RBC-binding kinetics, into high, medium and low binding activity. A correlation was detected between the high binding activity of a peptide and the presence of either a KEK motif (or its variants LEK or KEL) or a NVXAA (where X is V or Y). Peptides with medium or low binding activities did not possess either of these two consensus sequences. Selective modification of amino acids within the KEK motif diminished their uptake or binding capacity. Competitive inhibition assays of labeled or unlabeled peptide demonstrated a correlation between the presence of KEK or NVXAA motifs and a high binding activity of a peptide. Invasion-inhibition studies showed a direct correlation between a peptide's binding activity and inhibitions of human RBC reinvasion. Other experiments showed that high binding activity peptides show a decreased uptake with related and nonrelated human erythrocytes.

22 citations


Journal ArticleDOI
TL;DR: The results presented here indicate the existence of T- and B-cell epitopes within the MTP40 protein, added to the fact that it appears to be a species-specific antigen of M. tuberculosis, which may be useful in the design of more accurate diagnostic tests and an improved vaccine against human TBC.
Abstract: Synthetic peptides derived from the amino acid sequence of MTP40, a recently characterized Mycobacterium tuberculosis protein, were tested by two different immunological assays in 91 individuals. For the purposes of this study, the population was distributed in four groups: active tuberculosis (TBC) patients with elevated bacillus loads (BK+), active TBC patients with low bacillus loads (BK-), healthy individuals living in the same household with tuberculous patients (HH), and normal individuals, who had presumably never been in contact with the bacilli (control). We found that T cells of individuals belonging to the HH group showed the highest and most frequent recognition of these peptides in a T-cell proliferation assay, while their antibodies showed the lowest recognition of these peptides when tested by enzyme-linked immunosorbent assay. In contrast, TBC patients revealed an inverse pattern of immune response. Interestingly, one of these peptides (P7) was recognized by T cells of 64% of the HH individuals and by 4.5% of normal donors. Another peptide (P4) was recognized by 55% of sera from BK+ patients and by 5.5% of normal donors. The results presented here indicate the existence of T- and B-cell epitopes within the MTP40 protein. Given the particular recognition pattern of this protein, added to the fact that it appears to be a species-specific antigen of M. tuberculosis, a detailed study of the immune response to it may be useful in the design of more accurate diagnostic tests and an improved vaccine against human TBC.

22 citations