The influenza virus hemagglutinin (HA) is an envelope virus glycoprotein responsible for the attachment of the virus particles to cells via binding terminal sialic acid residues of cell surface oligosaccharides. In our previous works on influenza A virus escape mutants, that is, mutants resistant to the neutralization effect of monoclonal antibodies, we encountered amino acid changes in the vicinity of receptor-binding pocket of the HA. In this work the degree of the affinity to both alpha-2, -3, and alpha-2, -6, -sialoglycoconjugates was assessed for escape mutants of influenza H1 and H5 viruses. The data demonstrate that the decrease of the positive electrostatic charge of the HA molecule surface resulting from amino acid changes conferring resistance to monoclonal antibodies may lead to a lowering of the affinity to sialic acid-containing analogs of cell receptors. The results are discussed in the context of the evolution of HA in natural circulation of H1 and H5 influenza viruses.