How party dips can give you herpes

It’s usually not a party until the chips and dip rock up.

But, a new investigation has revealed that these tasty party treats can be hiding some very dangerous bacteria.

Norovirus, streptococcus – which gives you a sore throat – and herpes simplex – the cold sore virus, could all be lurking in your favourite dips.


The investigation revealed that if as little as one partygoer commits the ultimate party foul of ‘double dipping’, for the bacteria multiplying.

Microbiologists revealed on Monday’s episode of Food Unwrapped on Channel 4 that thousands of organisms live in the tiniest amount of saliva.

This means if someone double dips, the bacteria can transfer and multiply.

The experts also revealed the one crowd favourite that transfers the most bacteria.

Testing popular dips like taramasalata, houmous, and sour cream, it was revealed that the ‘runnier’ the dip, the easier is is for bacteria to multiply.

Matt Tebbutt, co-presenter of Food Unwrapped, double-dipped chips into all three dips and in just two hours, there was more than 100 times more bacteria in the pot of sour cream than an uncontaminated sample.

Bacteria also grew quickly in taramasalata, where there was 50 times more bacteria.

Tebbutt said, ‘If you are dip sharing, it’s the runniest dips you have to be aware of as they are more likely to drip back into the tub after they have been in your mouth, hence more bacteria.’

Food safety expert Jonathan France also revealed that if someone has a virus such as norovirus, streptococcus, or herpes simplex, you may catch their infection even if only a small amount of their saliva has contaminated a party dip.

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You’ve Never Seen Herpes Like This Before

Herpes is decidedly not amazing. But a new view of its molecular structure might make you say “wow.”

Two teams of scientists, one in China and another in the United States, have released new up-close views of the protein capsule that encompasses herpesvirus DNA, called a capsid. They revealed some of the best images yet of the virus (or of any large virus, for that matter). And it’s an important virus to study.

“A clear understanding of the structure and function of the various proteins of herpesvirus could help guide development of anti-viral agents as well as increase its utility and efficiency as a therapeutic agent for treating tumors,” author Xiangxi Wang from the Chinese Academy of Sciences told Gizmodo.

Below is his team’s new view of the herpes simplex virus 2 structure, along with a single unit of the whole capsid.


The herpes simplex virus 2 capsid, below, and a single unit, above. Graphic: Xiagxi Wang

Viruses are pretty incredible. Somehow, lots of individual protein pieces combine to form a capsule, like the hexagons and pentagons of a soccer ball or the triangles on a twenty sided die. Except in this case, it’s 3,000 or so of the same proteins arranged in a 200-nanometer ball—one of the largest viruses, but still incredibly tiny.

These capsids provide the container in which a virus’s genetic material is stored, which they release order to cause infection. In the case of herpes, that can include the familiar cold sores and genital herpes infections. But other viruses in the Herpesviridae family can cause encephalitis or even cancer.

The two teams of researchers used cryo-EM, or cryo electron microscopy, to take the image, according to a pair of new studies in the journal Science. The Nobel Prize-winning method involves freezing the molecule in such a way that it doesn’t crystallize, then bouncing electrons off of the object to determine its physical structure.

Others have imaged the herpesvirus before, but researchers could image these molecules down to 3.5 angstrom (0.35 nanometer) and 3.1 angstrom resolution—the best so far for a small virus. This revealed the identity of the individual building blocks that make up the proteins, the amino acids. They also found that these proteins aren’t all the same—slight differences could potentially supply some flexibility to the capsule.

As Tufts University researcher Ekaterina E. Heldwein, who was not involved in this study, pointed out in a commentary in the same issue of Science, neither group could resolve the portal by which DNA enters the capsule. Still, she said, these studies will be important for future investigation into the viruses’ structures.

Of course there’s an end goal here, said Wang: Creating drugs that could help treat these viruses.

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