Scientists solve a 30-year rye pollen mystery that could transform cancer research

 

Nearly 30 years ago, researchers discovered two unusual molecules in rye pollen that appeared to slow tumor growth in animal studies. Despite the promising findings, the research reached a dead end because scientists could not determine the molecules' exact three dimensional structures.

Now, chemists at Northwestern University have solved that long standing mystery. By constructing the molecules from scratch in the laboratory, they confirmed the precise structures of secalosides A and B for the first time.

With an accurate molecular blueprint available, researchers can now investigate how these compounds from rye pollen, which comes from a cereal crop widely grown for its grain, interact with the immune system. That knowledge could eventually help guide the development of new approaches to cancer treatment.

The findings were published in the Journal of the American Chemical Society.

"In preliminary studies, other researchers found that rye pollen could help different animal models clear tumors through some unknown, non-toxic mechanism," said Northwestern's Karl A. Scheidt, who led the study. "Now that we confirmed the structure of these molecules, we can find the active ingredient -- or what part of the molecule is doing the work. This is an exciting starting point to make better versions of these molecules that could possibly inform approaches to cancer therapy."

Scheidt is a professor of chemistry at Northwestern's Weinberg College of Arts and Sciences and a professor of pharmacology (by courtesy) at Northwestern University Feinberg School of Medicine. He also is a member of the Chemistry of Life Processes Institute and of the Robert H. Lurie Comprehensive Cancer Center of Northwestern University.

Nature's Role in Drug Discovery

Many important medicines have their roots in nature. Scientists have long studied plants, fungi, and microbes for compounds that can inspire new treatments.

Morphine, a powerful pain medication, comes from the opium poppy. Taxol, an important chemotherapy drug, was first isolated from the Pacific yew tree. Statins, which help lower cholesterol and reduce the risk of heart disease, originated from fungi.

"Natural products aren't necessarily effective drugs on their own, but they are great leads," Scheidt said. "We can find inspiration in natural products and use chemistry to make better versions that are orally available, survive the metabolism and hit the right targets."

Rye pollen could eventually join that list. Rye pollen extract is already sold as a dietary supplement that many people use to support prostate health. However, scientists have not yet developed it into a pharmaceutical treatment. A major obstacle was the lack of a clear picture of the molecules' three dimensional structures.

Solving a Decades Long Molecular Puzzle

Traditional techniques, including advanced nuclear magnetic resonance spectroscopy, could not fully determine how key parts of the molecules were arranged. As a result, scientists spent decades debating between two possible structural models.

Both versions contained the same atoms connected in the same way and shared the same overall shape. The difference was that one critical region existed as a mirror image in each model. Even that subtle variation can dramatically affect how a molecule interacts with biological targets and whether it produces a biological effect.

"It's like your hands," Scheidt said. "They are mirror images of each other, but you need a different glove for each. If you had two left-handed gloves, it wouldn't work because your hands can't be superimposed on top of one another."

Building the Molecules From Scratch

To resolve the uncertainty, the Northwestern team relied on total synthesis, a process in which researchers build a natural molecule step by step in the laboratory.

The work proved exceptionally difficult because secalosides A and B contain an extremely rare, highly strained 10 membered ring at their core. That tightly compressed structure is notoriously challenging to assemble.

The researchers overcame the problem by first creating a larger, more flexible ring. They then triggered a chemical reaction that converted it into the smaller strained ring in a single step.

After producing both proposed versions of the molecules, the team compared them with samples extracted from rye pollen. Only one matched perfectly, allowing the researchers to definitively identify the correct structures.

"We've demonstrated we can make the core of this natural product," Scheidt said. "Now, we're trying to find potential collaborators in immunology who could help us translate this to a possible clinical endpoint."

The study, "Synthesis and structural confirmation of secalosides A and B," was supported by the National Institute of General Medical Science, the Chemistry of Life Processes Institute Lambert Fellowship and the National Science Foundation.

Journal Reference:

1. Yunchan Nam, Anthony T. Tam, Troy E. Reynolds, Diego N. Rojas, Jonathan A. Brekan, Sneha Sil, Karl A. Scheidt. Synthesis and Structural Confirmation of Secalosides A and B. Journal of the American Chemical Society, 2025; 148 (1): 86 DOI: 10.1021/jacs.5c18864

Courtesy:

 Northwestern University. "Scientists solve a 30-year rye pollen mystery that could transform cancer research." ScienceDaily. ScienceDaily, 6 July 2026. <www.sciencedaily.com/releases/2026/06/260625014838.htm>. 

Scientists discover a completely different way to fight viruses

 

Scientists have uncovered a previously unknown way that sea anemones defend themselves against viruses, revealing that the evolution of animal immune systems may be far more diverse than previously believed. The newly identified defense relies on a protein that closely resembles one of the most important antiviral proteins in humans, yet performs the opposite function while still being essential for protecting the animal from infection. The findings suggest that evolution produced more than one successful strategy for fighting viruses across the animal kingdom.

The research, led by PhD candidate Ton Sharoni and Prof. Yehu Moran at the Hebrew University of Jerusalem in collaboration with scientists from the University of North Carolina at Charlotte, was published in Nature Ecology & Evolution. It challenges the long standing idea that animals inherited a single core antiviral system from a common ancestor and instead points to multiple evolutionary solutions for resisting viral infections.

An Ancient Animal Offers New Clues About Immunity

Viruses have threatened living organisms throughout evolutionary history. In humans and other vertebrates, one of the body's key antiviral defenses depends on a protein called MAVS. When a virus is detected, MAVS helps trigger the immune system so it can respond to the infection.

To investigate how old this defense system might be, the researchers studied sea anemones. These ancient marine animals split from the evolutionary line that eventually led to humans more than 600 million years ago. Because they are close relatives of corals and jellyfish, sea anemones provide scientists with a valuable glimpse into the early evolution of animal immunity.

During the study, the team discovered a previously unknown protein they named CARDIB (CARD Inhibitor Binding protein). At first, CARDIB looked remarkably similar to MAVS, leading researchers to believe it might perform the same antiviral role found in humans.

That assumption quickly fell apart.

"Everything about CARDIB suggested it should function like MAVS," said Prof. Yehu Moran, head of the Department of Ecology, Evolution and Behavior at the Hebrew University. "Instead, we discovered that it does the exact opposite. Rather than activating antiviral defenses, CARDIB normally suppresses them."

A Surprising Protein That Protects by Slowing the Immune System

The discovery immediately raised an important question. Why would an animal deliberately suppress its own immune response?

To find out, the researchers used CRISPR gene editing to remove the CARDIB gene from sea anemones before exposing them to viruses.

The results were unexpected. Sea anemones without CARDIB became much more susceptible to infection. Viruses multiplied more rapidly, the animals failed to properly activate their antiviral defenses, and their ability to fight infection dropped dramatically.

"The results were completely counterintuitive," said Sharoni. "Although CARDIB acts as a brake on the immune system under normal conditions, that brake turns out to be essential for mounting an effective antiviral response."

Overall, the experiments showed that sea anemones rely on an antiviral pathway that is fundamentally different from the one used by humans, even though both systems contain molecular components that look strikingly alike.

Natural Environment Confirms the Discovery

The researchers also wanted to determine whether this newly identified immune pathway mattered outside carefully controlled laboratory conditions.

To answer that question, genetically modified sea anemones were moved from laboratory aquaria into outdoor marine mesocosms supplied with natural estuarine water in South Carolina. This exposed the animals to the wide variety of viruses and microorganisms found in their normal environment.

The difference became obvious within days. Sea anemones lacking CARDIB and related antiviral genes accumulated substantially more viruses than unmodified animals. Researchers also found that one immune gene that appeared only moderately important in laboratory tests became clearly important under natural environmental conditions.

"This demonstrated that the pathway we discovered is not simply a laboratory phenomenon," said Moran. "It plays a crucial role in helping these animals cope with the viral challenges they face in nature."

Multiple Evolutionary Solutions to Fighting Viruses

The findings suggest that evolution did not settle on a single universal antiviral strategy. Instead, different groups of animals may have independently developed distinct molecular systems for detecting viruses and preventing them from spreading.

"Humans and sea anemones both need protection from viruses, but this work shows that evolution can organize those defenses in fundamentally different ways," Moran added.

The research also underscores the importance of looking beyond traditional laboratory animals. Ancient organisms such as sea anemones can preserve evolutionary innovations that would remain hidden if scientists focused only on humans, mice, and other commonly studied species.

As researchers continue exploring the remarkable diversity of life, discoveries like this are revealing that evolution has repeatedly found unexpected ways to solve some of biology's most fundamental challenges.

Journal Reference:

1. Ton Sharoni, Adrian Jaimes-Becerra, Sydney Birch, Hee-Jin Kwak, Daria Aleshkina, Magda Lewandowska, Joachim M. Surm, Hannah Justin, Reuven Aharoni, Adam M. Reitzel, Yehu Moran. An ancient anthozoan protein reveals an alternative evolutionary path of antiviral signalling. Nature Ecology, 2026; DOI: 10.1038/s41559-026-03112-3

Courtesy:

The Hebrew University of Jerusalem. "Scientists discover a completely different way to fight viruses." ScienceDaily. ScienceDaily, 30 June 2026. <www.sciencedaily.com/releases/2026/06/260630020534.htm>.