Abstract:
:We have isolated a series of five proteins which appear to possess characteristic individual capacities for synthesizing dextrans and binding dextrans. Our suggestion that these proteins comprise an isozyme-like distribution of lectin and enzyme activities is, of course, very speculative and remains to be rigourously confirmed. However, the very identification of these several dextran binding proteins provides a biochemical basis to explain numerous observations suggesting that more than one mechanism for dextran binding is possessed by S. mutans (for instance: 24-27), especially the observations with mutants (24). These proteins probably are the molecular determinants of host infection by S. mutans and may prove to be potent immunogens for use in a vaccine. The presence of a dextran-binding lectin in S. mutans implicates this bacterial lectin in the earliest stage of infection: Attachment to host tissues. The multiplicity of proteins possessing characteristic dextran-synthesizing and dextran-binding capacities indicates the complexity of the adherence mechanisms evolved in S. mutans. Experiments with other bacteria (10-12, 28) suggest that bacterial lectins, in concert with host tissue carbohydrates, may be the molecular mediators of host recognition and subsequent initial attachment of bacterial cells to host tissues in non-pathogenic as well as pathogenic bacteria.
journal_name
Adv Exp Med Bioljournal_title
Advances in experimental medicine and biologyauthors
McCabe MM,Hamelik RMdoi
10.1007/978-1-4684-3369-2_84subject
Has Abstractpub_date
1978-01-01 00:00:00pages
749-59eissn
0065-2598issn
2214-8019journal_volume
107pub_type
杂志文章abstract::The continuous part of a hybrid (pulse-modulated) model of testosterone (Te) feedback regulation in the human male is extended with infinite-dimensional and nonlinear blocks, to obtain the dynamics that better agree with the hormone concentration profiles observed in clinical data. A linear least-squares based optimiz...
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