Scientists discover glow-in-the-dark shark in Pacific

Scientists have discovered new species of glow-in-the-dark shark living 1,000 feet below the Pacific Ocean off the coast of the northwestern Hawaiian islands.

It has been named Etmopterus lailae and belongs to lanternshark family.

It has an unusually large nose, weighs a little less than a kilo and measures less than a foot.

This unique features and characteristics make it different form other lanternsharks.

Key Facts

Etmopterus lailae has a strange head shape which is large and bulgy snout where its nostrils and olfactory organs are located.

It dwells in a deep sea environment with almost no light so it has big sniffer to find food.

It has flank markings that go forward and backward on their bellies and a naked patch without scales on the underside of its snout.

Like other lanternsharks, it is also bio-luminescent. Its flanks on the bottom of its belly glow in the dark.

The markings on its belly and tail also are specific to it. This species is understudied because of its size and the fact that it lives in very deep water.

It is not easily visible or accessible like so many other sharks.

Human antibodies produced in lab for first time

Scientists for the first time have produced human antibodies in the laboratory.
They have developed revolutionary technique which can help in rapid development of new vaccines to treat a wide range of infectious diseases.
Antibodies Antibodies mainly function in the humoral adaptive immune system by secreting antibodies to fight off infections caused by bacteria, viruses, and other invasive pathogens.
They are produced by body’s B cells (B lymphocytes). When an individual B cell recognises a specific pathogen-derived antigen molecule, it proliferates and develops into plasma cells that secrete large amounts of antibody capable of binding to the antigen and fending off the infection.
Key Facts To develop revolutionary technique, researchers had replicated the process of natural production of antibodies from B cells isolated from patient blood samples in the laboratory to produce specific antibodies.
They had found that B cells need a second signal to start proliferating and developing into plasma cells apart encountering a specific antigen at first instance.
For the second signal they used short DNA fragments called CpG oligonucleotides, which activate a protein named TLR9 inside B cells.
However, they found that treating patient-derived B cells with CpG oligonucleotides stimulates every B cell, not just the tiny fraction capable of producing a particular antibody.
So to overcome the problem they treated patient-derived B cells with tiny nanoparticles coated with both CpG oligonucleotides and an antigen.
With this technique, CpG oligonucleotides were only internalised into B cells recognising the specific antigen.
These cells were only ones in which TLR9 is activated to induce their proliferation and development into antibody-secreting plasma cells.
Significance Researchers successfully demonstrated their approach using various bacterial and viral antigens, including the tetanus toxoid and proteins from several strains of influenza A.
In each case, they were able to produce specific, high-affinity antibodies in just a few days.
In some of the anti-influenza antibodies generated by the technique were able to neutralise multiple strains of the virus.
They were able to generate anti-HIV antibodies from B cells isolated from HIV-free patients.
This approach may help researchers to rapidly generate therapeutic antibodies for the treatment of infectious diseases and other conditions such as cancer.

Scientists develop super-flexible and strong artificial silk

Scientists from the University of Cambridge have developed super-stretchy and strong artificial (synthetic) spider silk, almost entirely composed of water.

The synthetic spider silk mimics properties of spider silk, one of nature’s strongest materials for a range of applications such as making eco-friendly textiles and sensors.

Composition The fibres of the synthetic spider silk are spun from hydrogel, a soupy material which is 98% water.

The remaining 2% of the hydrogel is made of naturally available silica and cellulose.

These materials are held together in a network by barrel-shaped molecular “handcuffs” known as cucurbiturils.

The chemical interactions between the different components enable to pull long fibres from the gel.

The water from hydrogel evaporates after it is stretched for 30 seconds, leaving a strong fibre which is both strong and stretchy.

Properties The fibres of the synthetic spider silk are extremely thin threads and are of few millionths of a metre in diameter.

They resemble miniature bungee cords and can absorb large amounts of energy. They are sustainable, non-toxic, less energy-intensive and can be made at room temperature.

The fibres are capable of self-assembly at room temperature, and are held together by supramolecular host, where atoms share electrons.

They can support stresses in the range of 100 to 150 megapascals, which is similar to other synthetic and natural silks.