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Unlikely unfolding of gpV-like proteins cautions against membrane-disruption models; extends beta-helical structural data but leaves functional mechanisms open.
Poster Sessions C410 chain forming the beta-helices are very different.Nevertheless, gpV, gp138 and PA0616 are water soluble and SDS-resistant proteins and show no obvious membrane affinity.They are unlikely to unfold upon interaction with the membrane during phage attachment.GpV, gp138 and PA0616 contain a conserved cluster of histidines at the tip of the beta-helical domain.These histidines bind a Fe atom in the octahedral configuration.In addition to Fe, gpV also contains Ca and Cl near the spike's apex.The peculiar topology and thermodynamic stability of gpV, gp138 and PA0616 suggests that these proteins are used as rigid and sharp needles to breach the outer membrane of the host cell using the energy of the contractile sheath.These spikes appear to create an opening in the host cell membrane into which the tail tube in inserted for subsequent DNA release into the host cell.
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Vives-Adrián et al. (2011) studied this question.
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