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Biomedical subjects

H T Wright

Publications and source records attributed to H T Wright.

76 records · Page 5Linked to original sources
PubMed1966

Congenital anomalies and viral infections in infants. The etiologic role of maternal viral infections.

Some viruses, such as rubella and human cytomegalovirus, are known to cross the placental barrier and infect the fetus. In other cases of maternal viral infections, such as herpes simplex, evidence for transplacental passage is less convincing and fetal damage or neonatal disease may be coincidental or associated with perinatal infection. Certain cases of fetal or neonatal disease following maternal viral infections may be associated with disease in the mother which affects her metabolic processes or the placenta in such a way as to interfere with development of the fetus and infant. The possible effects of transplacental viral infections are several. Fetal loss may occur by means of abortion or stillbirth. There may be infection of the fetus, with clinical manifestations such as rash, or without clinical manifestations. The infant may be born with congenital defects, including such deformities as cataracts, cardiac anomalies, mental retardation or cerebral palsy. Although a number of maternal viral diseases have been etiologically incriminated in congenital defects, only two-rubella and cytomegalovirus infection-are definitely proved to be associated with anomalies or mental retardation in infants.

Congenital Abnormalities↗
PubMedDate not supplied

Evolution of the multidomain protein wheat germ agglutinin.

We compared the homologous amino acid sequences of hevein and each of the four domains (A, B, C, and D) of wheat germ agglutinin and used them to construct a pseudophylogenetic tree relating these sequences to a hypothetical common ancestor sequence. In the crystal structure of the wheat germ agglutinin dimer, six pseudo-two-fold rotational symmetry axes have previously been located in addition to the true twofold axis. Four of these relate two nonidentical domains to each other in each of the four possible pairs constituting the sugar-binding sites (A1D2, A2D1, B1C2, and B2C1). The remaining two relate contiguous unique pairs of sugar-binding sites to each other (A1D2 to B1C2, and A2D1 to B2C1). These latter two sets of pairs are related to each other by the true twofold axis. Side chains that mediate sugar binding in the interfaces of each of the four pairs were found to be largely conserved. The sequence homology, taken together with these pseudo-symmetry elements in the dimer structure, suggests a pathway for the evolution of the four-domain molecule from a single-domain dimer that can be correlated with simultaneous development of the saccharide-binding sites.

Amino Acid Sequence↗