How the Malevolent Designer Beats Medical Science

H3N2 influenza virus particles, coloured transmission electron micrograph (TEM). Each virus consists of a nucleocapsid (protein coat) that surrounds a core of RNA (ribonucleic acid) genetic material. Surrounding the nucleocapsid is a lipid envelope that contains the glycoprotein spikes haemagglutinin (H) and neuraminidase (N). These viruses were part of the Hong Kong Flu pandemic of 1968-1969 that killed approximately one million worldwide. H3N2 viruses are able to infect birds and mammals as well as humans. They often cause more severe infections in the young and elderly than other flu strains and can lead to increases in hospitalisations and deaths.

Credit: CDC / SCIENCE PHOTO LIBRARY

Fast-Spreading Mutation Helps Common Flu Subtype Escape Immune Response - 2020 - News Releases - News - Johns Hopkins Bloomberg School of Public Health

News today of how creationism's malevolent designer keeps ahead of medical science by giving the common influenza virus H3N2 strain a mutation that makes it immune to human antibodies by preventing our antibodies from binding to a protein on the viral coat.

Additionally, the mutation makes the virus so good at spreading that it is now present in virtually all strains of H3N2.

The study was conducted by two researchers at Johns Hopkins Bloomberg School of Public Health and is published open access a few days ago in the online journal PLOS Pathogens:

Abstract

In the 2014–2015 influenza season a novel neuraminidase (NA) genotype was detected in global human influenza A surveillance. This novel genotype encoded an N-linked glycosylation site at position 245–247 in the NA protein from clade 3c.2a H3N2 viruses. In the years following the 2014–2015 season, this novel NA glycosylation genotype quickly dominated the human H3N2 population of viruses. To assess the effect this novel N-linked glycan has on virus fitness and antibody binding, recombinant viruses with (NA Gly+) or without (NA Gly-) the 245 NA glycan were created. Viruses with the 245 NA Gly+ genotype grew to a significantly lower infectious virus titer on primary, differentiated human nasal epithelial cells (hNEC) compared to viruses with the 245 NA Gly- genotype, but growth was similar on immortalized cells. The 245 NA Gly+ blocked human and rabbit monoclonal antibodies that target the enzymatic site from binding to their epitope. Additionally, viruses with the 245 NA Gly+ genotype had significantly lower enzymatic activity compared to viruses with the 245 NA Gly- genotype. Human monoclonal antibodies that target residues near the 245 NA glycan were less effective at inhibiting NA enzymatic activity and virus replication of viruses encoding an NA Gly+ protein compared to ones encoding NA Gly- protein. Additionally, a recombinant H6N2 virus with the 245 NA Gly+ protein was more resistant to enzymatic inhibition from convalescent serum from H3N2-infected humans compared to viruses with the 245 NA Gly- genotype. Finally, the 245 NA Gly+ protected from NA antibody mediated virus neutralization. These results suggest that while the 245 NA Gly+ decreases virus replication in hNECs and decreases enzymatic activity, the 245 NA glycan blocks the binding of monoclonal and human serum NA specific antibodies that would otherwise inhibit enzymatic activity and virus replication.

Author summary

Influenza virus infects millions of people worldwide and leads to thousands of deaths and millions in economic loss each year. During the 2014/2015 season circulating human H3N2 viruses acquired a novel mutation in the neuraminidase (NA) protein. This mutation has since fixed in human H3N2 viruses. This mutation at position 245 through 247 in the amino acid sequence of NA encoded an N-linked glycosylation. Here, we studied how this N-linked glycan impacts virus fitness and protein function. We found that this N-linked glycan on the NA protein decreased viral replication fitness on human nasal epithelial cells (hNEC) but not immortalized Madin-Darby Canine Kidney (MDCK) cells. We also determined this glycan decreases NA enzymatic activity, enzyme kinetics and affinity for substrate. Furthermore, we show that this N-linked glycan at position 245 blocks some NA specific inhibitory antibodies from binding to the protein, inhibiting enzymatic activity, and inhibiting viral replication. Finally, we showed that viruses with the novel 245 N-linked glycan are more resistant to convalescent human serum antibody mediated enzymatic inhibition. While this 245 N-linked Glycan decreases viral replication and enzymatic activity, the 245 N-linked glycan protects the virus from certain NA specific inhibitory antibodies. Our study provides new insight into the function of this dominant H3N2 NA mutation and how it impacts antigenicity and fitness of circulating H3N2 viruses.

Powell H, Pekosz A (2020)
Neuraminidase antigenic drift of H3N2 clade 3c.2a viruses alters virus replication, enzymatic activity and inhibitory antibody binding.
PLoS Pathog 16(6): e1008411. https://doi.org/10.1371/journal.ppat.1008411

Copyright: © 2020 The Authors
Open access
Reprinted under a Creative Commons Attribution 4.0 International Licence (CC BY 4.0)

This discovery presents a number of problems for intelligent [sic] design creationists:

• The way creationists normally explain away these instances of what can only be described as malevolence on the part of any designer, is by invoking the religious notion of 'The Fall', so rendering any claim that ID is science not religion, redundant and patently false. No science would invoke mythology and a magic sky man in any explanation because those are unproven and unfalsifiable notions, so have no place in a scientific explanation.
• If they invoke 'micro-evolution' (i.e. evolution) then what we have here is an example of a mutation which is clearly beneficial, yet the currently in vogue notion in creationism is that all mutations are detrimental and so should be deleterious (a notion called genetic entropy, again related to the religious notion of 'The Fall'). But very clearly the evidence shows how this mutation very quickly spread within the viral gene-pool because it gives carriers an advantage.
• Abandoning the pretense that ID is not religion, as many creationists now have, leaving no doubt that the putative designer is none other than the Abrahamic god, raises the question of why a supposedly omnibenevolent god would act like a malevolent, psychopath who makes people sick and die for the fun of it.

Just as with Covid-19, currently devastating human society world-wide and causing untold economic damage as well as killing millions, it is a major embarrassment to creationists that the only explanation that doesn't leave their god looking like a malevolent, anthropophobic psychopath is evolution - the rejection of which is the reason so many are creationists in the first place.

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