Wal-Mart Stores on Monday said it has completed the acquisition of internet retailer Jet.com after agreeing to pay about $3 billion for the e-commerce startup last month.
Wal-Mart Chief Executive Doug McMillon announced the closing of the deal, which was pending regulatory approval, in a blog post on the retailer’s website.
The acquisition will impact Wal-Mart’s 2017 fiscal year earnings marginally more than the retailer’s initial estimate of a 5 cents per share impact as the transaction closed ahead of time, Wal-Mart said.
The deal, which was the largest for an online startup, will give Wal-Mart
access to Jet.com’s innovative pricing software and will help the Bentonville, Arkansas-based retailer to better compete with online rival Amazon.com
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“A lot of folks ask me ‘Why Jet.com?,” McMillon said in a blog post. The answer he said was in the savings both Wal-Mart and Jet can together offer shoppers.
Jet, with its ability to lower prices as customers add more items to their shopping carts, will help the world’s largest retailer reach more customers such as millennial shoppers. The deal would also strengthen Wal-Mart’s existing e-commerce infrastructure, McMillon said.
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Wal-Mart has built its website into the second largest online retailer by traffic in the U.S. in the past six months, the blog post said. It has also expanded the assortment of products on its website from 7 million to 15 million items and is adding a million more each month.
Jet’s founder Marc Lore will join Wal-Mart as the President and Chief Executive of Wal-Mart’s U.S. ecommerce business and will report to McMillon, the company said in a separate statement.
“I’ll be spending a lot of time with the team in the coming weeks and months focused on scaling Walmart.com and Jet.com,” Lore said.
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Over a five-year period Lore will receive stock units that involve the issuance of 3.55 million shares of Wal-Mart’s common stock valued at 10 cents per share, the statement said. This is a part of the $300 million of Wal-Mart shares that would be paid over time as part of the original transaction.
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In late 2015, the first example of a transferrable polymyxin resistance mechanism in Gram-negative pathogens, MCR-1, was reported. Since that report, MCR-1 has been described to occur in many Gram-negative pathogens, and the mechanism of MCR-1-mediated resistance was rapidly determined: an ethanolamine is attached to lipid A phosphate groups, rendering the membrane more electropositive and repelling positively charged polymyxins. Acquisition of MCR-1 is clinically significant because polymyxins are frequently last-line antibiotics used to treat extensively resistant organisms, so acquisition of this mechanism might lead to pan-resistant strains. Therefore, the ability to inhibit MCR-1 and restore polymyxin sensitivity would be an important scientific advancement. Peptide-conjugated phosphorodiamidate morpholino oligomers (PPMOs) are antisense molecules that were designed to target mRNA, preventing translation. Peptide conjugation enhances cellular entry, but they are positively charged, so we tested our lead antibacterial PPMOs by targeting an essential Escherichia coli gene, acpP , and demonstrated that they were still effective in mcr - 1 -positive E.coli strains. We then designed and synthesized two PPMOs targeted to mcr-1 mRNA. Five clinical mcr-1 -positive E.coli strains were resensitized to polymyxins by MCR-1 inhibition, reducing MICs 2- to 16-fold. Finally, therapeutic dosing of BALB/c mice with MCR-1 PPMO combined with colistin in a sepsis model reduced morbidity and bacterial burden in the spleen at 24h and offered a survival advantage out to 5days. This is the first example of a way to modulate colistin resistance with an antisense approach and may be a viable strategy to combat this globally emerging antibiotic resistance threat.
IMPORTANCE Polymyxin use has been increasing as a last line of defense against Gram-negative pathogens with high-level resistance mechanisms, such as carbapenemases. The recently described MCR-1 is a plasmid-mediated mechanism of resistance to polymyxins. MCR-1 is currently found in Gram-negative organisms already possessing high-level resistance mechanisms, leaving clinicians few or no antibacterial options for infections caused by these strains. This study utilizes antisense molecules that target mRNA, preventing protein translation. Herein we describe antisense molecules that can be directly antibacterial because they target genes essential to bacterial growth or blockade of MCR-1, restoring polymyxin sensitivity. We also demonstrate that MCR-1 antisense molecules restore the efficacies of polymyxins in mouse models of E.coli septicemia. Considering all things together, we demonstrate that antisense molecules may be effective therapeutics either alone when they target an essential gene or combined with antibiotics when they target specific resistance mechanisms, such as those seen with MCR-1.
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