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While parental H5 HA exhibited limited binding to human tracheal epithelium, introduction of selected mutations converted the binding profile to that of a current human influenza strain HA.
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Figure 1 Effects of silica particle size on binding to human plasma proteins.
Figure 3 Effects of surface modification of silica particles on binding to human plasma proteins.
This construct shows significantly reduced binding to human netrin-1 (Fig. 1B).
Radiotracer binding to human carotid plaques was evaluated by in vitro autoradiography.
Binding to human RBCs was estimated after in vitro incubation of the compounds with whole blood.
Staining of Alb58 HA on human upper respiratory tracheal tissue sections revealed extensive binding of the protein to the apical side (Figure 1B) and thus correlated with its high affinity binding to human receptors.
The optimized Fc domain shows increased binding to human C1q.
Exposure to 0.2 ppm O3 markedly increased adhesion of polymorphonuclear leukocytes (PMNs) to human tracheal epithelial cells (Tosi et al. 1994).
By analysis of codon usage required to generate mutants capable of SA switching, we found that two or more simultaneous nucleotide changes are required to adapt the H5 HA gene for efficient binding to cells of the human tracheal epithelium.
There was no significant binding to normal tracheal epithelial cell outgrowths.
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