An aminoglycoside family of antibiotics was recently reported to partially correct the effect of nonsense mutations by specifically recognizing ribosomes and by promoting a readthrough mechanism for the modulation of translation and miscoding. The binding of aminoglycosides to ribosomes also enhances the ability of releasing factors, such as RF1 and RF2, to stabilize the nascent protein strand in the ribosome for further elongation. Furthermore, the expression of various gene products associated with the translational machinery can be regulated by treating cells with aminoglycoside antibiotics. Consequently, aminoglycoside antibiotics have been found to allow ribosomes to readthrough inappropriately inserted stop codon mutations in both human and animal models. The mechanism of translation termination is highly conserved among most organisms and is almost always signaled by an amber, ochre, or opal termination codon. By reducing the accuracy of translation, aminoglycosides increase the frequency of erroneous insertions at the nonsense codon and permit translation to continue to the end of the gene. Aminoglycoside antibiotics usually insert glutamine at nonsense UAG or UAA or tryptophan at nonsense UGA sites albeit at extremely modest efficiencies of the affected genes. Indeed, patients suffering from different heritable diseases, such as cystic fibrosis, muscular dystrophies, hemophilia, lysosomal storage disorder or ataxia telangiectasia due to stop codon mutations experienced clinical and laboratory improvement after gentamicin treatment. For example, expression of full-length CFTR protein at the apical cell membrane was observed in cystic fibrosis patients. Moreover, suppression of stop mutations in the CFTR gene by parenteral gentamicin could be predicted in-vitro. These clinical studies paved the way to the development of orally bioavailable small molecule modality that is designed to induce ribosomes to selectively read through some premature stop codons during mRNA translation, however, raised some controversies regarding its application in other premature stop codons. We describe here a novel premature termination codon in the CD18 gene causing severe LAD1 phenotype in two Palestinian children. We investigated the in-vivo and Sorafenib 284461-73-0 in-vitro effects of gentamicin-induced readthrough in the CD18 protein of these patients. We also show the effect of gentamicin treatment on the expression of CD11 molecules and their interaction with CD18 at the cell surface. Nonsense mutations have rarely been described in the CD18 gene. This type of mutation was reported to correlate with a severe clinical phenotype in other primary immunodeficiencies, such as Wiskott-Aldrich syndrome,, as well as in nonimmunodeficiency inherited diseases.