Title : An amino acid substitution in PBP-3 in Haemophilus influenzae associate with the invasion to bronchial epithelial cells.

Pub. Date : 2010

PMID : 18417334






3 Functional Relationships(s)
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1 We examined whether beta-lactamase-negative ampicillin-resistant (BLNAR) strains that are known to have ampicillin resistance due to a substitution of amino acid of penicillin binding protein (PBP)-3, differ from beta-lactamase-negative ampicillin-susceptible strains with regard to invasion of bronchial epithelium. Ampicillin phosphatidylethanolamine binding protein 1 Homo sapiens
2 We examined whether beta-lactamase-negative ampicillin-resistant (BLNAR) strains that are known to have ampicillin resistance due to a substitution of amino acid of penicillin binding protein (PBP)-3, differ from beta-lactamase-negative ampicillin-susceptible strains with regard to invasion of bronchial epithelium. Ampicillin phosphatidylethanolamine binding protein 1 Homo sapiens
3 We examined whether beta-lactamase-negative ampicillin-resistant (BLNAR) strains that are known to have ampicillin resistance due to a substitution of amino acid of penicillin binding protein (PBP)-3, differ from beta-lactamase-negative ampicillin-susceptible strains with regard to invasion of bronchial epithelium. Ampicillin phosphatidylethanolamine binding protein 1 Homo sapiens